1okw - Revision history

OCA at 12:44, 13 December 2023

OCA — Wed, 13 Dec 2023 12:44:39 GMT

←Older revision		Revision as of 12:44, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1okw' size='340' side='right'caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1okw' size='340' side='right'caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=ACE:ACETYL+GROUP'~~>~~ACE</scene>, <scene name='pdbligand=FCL:3~~-~~CHLORO-L-PHENYLALANINE'>FCL</scene>~~, ~~<scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [https://pdbe.org/1okw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [https://www.ebi.ac.uk/pdbsum/1okw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [https://pdbe.org/1okw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [https://www.ebi.ac.uk/pdbsum/1okw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CDK2_HUMAN CDK2_HUMAN]] Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization.<ref>PMID:10499802</ref> <ref>PMID:11051553</ref> <ref>PMID:10995386</ref> <ref>PMID:10995387</ref> <ref>PMID:10884347</ref> <ref>PMID:11113184</ref> <ref>PMID:15800615</ref> <ref>PMID:18372919</ref> <ref>PMID:20147522</ref> <ref>PMID:20079829</ref> <ref>PMID:20935635</ref> <ref>PMID:20195506</ref> <ref>PMID:19966300</ref> <ref>PMID:21262353</ref> <ref>PMID:21596315</ref> <ref>PMID:21319273</ref> <ref>PMID:17495531</ref> ~~[[https://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.~~	+	[https://www.uniprot.org/uniprot/CDK2_HUMAN CDK2_HUMAN] Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization.<ref>PMID:10499802</ref> <ref>PMID:11051553</ref> <ref>PMID:10995386</ref> <ref>PMID:10995387</ref> <ref>PMID:10884347</ref> <ref>PMID:11113184</ref> <ref>PMID:15800615</ref> <ref>PMID:18372919</ref> <ref>PMID:20147522</ref> <ref>PMID:20079829</ref> <ref>PMID:20935635</ref> <ref>PMID:20195506</ref> <ref>PMID:19966300</ref> <ref>PMID:21262353</ref> <ref>PMID:21596315</ref> <ref>PMID:21319273</ref> <ref>PMID:17495531</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Transferase~~]]	+	[[Category: Synthetic construct]]
-	[[Category: Andrews, M]]	+	[[Category: Andrews M]]
-	[[Category: Cowan, A]]	+	[[Category: Cowan A]]
-	[[Category: Fischer, P]]	+	[[Category: Fischer P]]
-	[[Category: Green, S]]	+	[[Category: Green S]]
-	[[Category: Griffiths, G]]	+	[[Category: Griffiths G]]
-	[[Category: Innes, L]]	+	[[Category: Innes L]]
-	[[Category: Kontopidis, G]]	+	[[Category: Kontopidis G]]
-	[[Category: Lane, D]]	+	[[Category: Lane D]]
-	[[Category: McInnes, C]]	+	[[Category: McInnes C]]
-	[[Category: Paterson, D]]	+	[[Category: Paterson D]]
-	[[Category: Plater, A]]	+	[[Category: Plater A]]
-	[[Category: Powers, H]]	+	[[Category: Powers H]]
-	[[Category: Walkinshaw, M]]	+	[[Category: Walkinshaw M]]
-	[[Category: Zheleva, D]]	+	[[Category: Zheleva D]]
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Cyclin some]]~~	+
-	~~[[Category: Ligand exchange]]~~	+
-	~~[[Category: Peptidomimetic]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 10:51, 6 April 2022

OCA — Wed, 06 Apr 2022 10:51:24 GMT

←Older revision		Revision as of 10:51, 6 April 2022
Line 3:		Line 3:
	<StructureSection load='1okw' size='340' side='right'caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1okw' size='340' side='right'caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1OKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Transferase Transferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [~~http~~://pdbe.org/1okw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1okw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [https://pdbe.org/1okw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [https://www.ebi.ac.uk/pdbsum/1okw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CDK2_HUMAN CDK2_HUMAN]] Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization.<ref>PMID:10499802</ref> <ref>PMID:11051553</ref> <ref>PMID:10995386</ref> <ref>PMID:10995387</ref> <ref>PMID:10884347</ref> <ref>PMID:11113184</ref> <ref>PMID:15800615</ref> <ref>PMID:18372919</ref> <ref>PMID:20147522</ref> <ref>PMID:20079829</ref> <ref>PMID:20935635</ref> <ref>PMID:20195506</ref> <ref>PMID:19966300</ref> <ref>PMID:21262353</ref> <ref>PMID:21596315</ref> <ref>PMID:21319273</ref> <ref>PMID:17495531</ref> [[~~http~~://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.	+	[[https://www.uniprot.org/uniprot/CDK2_HUMAN CDK2_HUMAN]] Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization.<ref>PMID:10499802</ref> <ref>PMID:11051553</ref> <ref>PMID:10995386</ref> <ref>PMID:10995387</ref> <ref>PMID:10884347</ref> <ref>PMID:11113184</ref> <ref>PMID:15800615</ref> <ref>PMID:18372919</ref> <ref>PMID:20147522</ref> <ref>PMID:20079829</ref> <ref>PMID:20935635</ref> <ref>PMID:20195506</ref> <ref>PMID:19966300</ref> <ref>PMID:21262353</ref> <ref>PMID:21596315</ref> <ref>PMID:21319273</ref> <ref>PMID:17495531</ref> [[https://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:59, 1 July 2020

OCA — Wed, 01 Jul 2020 07:59:45 GMT

←Older revision		Revision as of 07:59, 1 July 2020
Line 1:		Line 1:

	==Cyclin A binding groove inhibitor Ac-Arg-Arg-Leu-Asn-(m-Cl-Phe)-NH2==		==Cyclin A binding groove inhibitor Ac-Arg-Arg-Leu-Asn-(m-Cl-Phe)-NH2==
-	<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='1okw' size='340' side='right'caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1OKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://pdbe.org/1okw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://pdbe.org/1okw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Cyclin\|Cyclin]]	+	*[[Cyclin 3D structures\|Cyclin 3D structures]]
-	*[[Cyclin-dependent kinase\|Cyclin-dependent kinase]]	+	*[[Cyclin-dependent kinase 3D structures\|Cyclin-dependent kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Andrews, M]]		[[Category: Andrews, M]]

OCA at 09:30, 26 September 2018

OCA — Wed, 26 Sep 2018 09:30:45 GMT

←Older revision		Revision as of 09:30, 26 September 2018
Line 3:		Line 3:
	<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/1okw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/1okw_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 38:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Andrews, M]]		[[Category: Andrews, M]]

OCA at 14:30, 22 December 2016

OCA — Thu, 22 Dec 2016 14:30:30 GMT

←Older revision		Revision as of 14:30, 22 December 2016
Line 1:		Line 1:
-	==~~CYCLIN~~ A ~~BINDING GROOVE INHIBITOR AC~~-~~ARG~~-~~ARG~~-~~LEU~~-~~ASN~~-(M-CL-~~PHE~~)-NH2==	+
		+	==Cyclin A binding groove inhibitor Ac-Arg-Arg-Leu-Asn-(m-Cl-Phe)-NH2==
	<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Human Human]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://pdbe.org/1okw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://pdbe.org/1okw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1okw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Andrews, M]]		[[Category: Andrews, M]]
Line 47:		Line 47:
	[[Category: Kontopidis, G]]		[[Category: Kontopidis, G]]
	[[Category: Lane, D]]		[[Category: Lane, D]]
-	[[Category: ~~Mcinnes~~, C]]	+	[[Category: McInnes, C]]
	[[Category: Paterson, D]]		[[Category: Paterson, D]]
	[[Category: Plater, A]]		[[Category: Plater, A]]

OCA at 09:56, 8 February 2016

OCA — Mon, 08 Feb 2016 09:56:13 GMT

←Older revision		Revision as of 09:56, 8 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1okw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Cell division protein kinase\|Cell division protein kinase]]
	*[[Cyclin\|Cyclin]]		*[[Cyclin\|Cyclin]]
		+	*[[Cyclin-dependent kinase\|Cyclin-dependent kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:26, 10 September 2015

OCA — Thu, 10 Sep 2015 10:26:03 GMT

←Older revision		Revision as of 10:26, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://pdbe.org/1okw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1okw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Cell division protein kinase 2\|Cell division protein kinase 2]]	+	*[[Cell division protein kinase\|Cell division protein kinase]]
	*[[Cyclin\|Cyclin]]		*[[Cyclin\|Cyclin]]
	== References ==		== References ==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Transferase]]
	[[Category: Andrews, M]]		[[Category: Andrews, M]]
	[[Category: Cowan, A]]		[[Category: Cowan, A]]

OCA at 22:29, 24 December 2014

OCA — Wed, 24 Dec 2014 22:29:23 GMT

←Older revision		Revision as of 22:29, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CDK2_HUMAN CDK2_HUMAN]] Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization.<ref>PMID:10499802</ref> <ref>PMID:11051553</ref> <ref>PMID:10995386</ref> <ref>PMID:10995387</ref> <ref>PMID:10884347</ref> <ref>PMID:11113184</ref> <ref>PMID:15800615</ref> <ref>PMID:18372919</ref> <ref>PMID:20147522</ref> <ref>PMID:20079829</ref> <ref>PMID:20935635</ref> <ref>PMID:20195506</ref> <ref>PMID:19966300</ref> <ref>PMID:21262353</ref> <ref>PMID:21596315</ref> <ref>PMID:21319273</ref> <ref>PMID:17495531</ref> [[http://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Andrews, M.]]	+	[[Category: Andrews, M]]
-	[[Category: Cowan, A.]]	+	[[Category: Cowan, A]]
-	[[Category: Fischer, P.]]	+	[[Category: Fischer, P]]
-	[[Category: Green, S.]]	+	[[Category: Green, S]]
-	[[Category: Griffiths, G.]]	+	[[Category: Griffiths, G]]
-	[[Category: Innes, L.]]	+	[[Category: Innes, L]]
-	[[Category: Kontopidis, G.]]	+	[[Category: Kontopidis, G]]
-	[[Category: Lane, D.]]	+	[[Category: Lane, D]]
-	[[Category: Mcinnes, C.]]	+	[[Category: Mcinnes, C]]
-	[[Category: Paterson, D.]]	+	[[Category: Paterson, D]]
-	[[Category: Plater, A.]]	+	[[Category: Plater, A]]
-	[[Category: Powers, H.]]	+	[[Category: Powers, H]]
-	[[Category: Walkinshaw, M.]]	+	[[Category: Walkinshaw, M]]
-	[[Category: Zheleva, D.]]	+	[[Category: Zheleva, D]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Cyclin some]]		[[Category: Cyclin some]]

OCA at 13:25, 28 September 2014

OCA — Sun, 28 Sep 2014 13:25:14 GMT

←Older revision		Revision as of 13:25, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1okw.~~png~~\|~~left~~\|200px]]	+	==CYCLIN A BINDING GROOVE INHIBITOR AC-ARG-ARG-LEU-ASN-(M-CL-PHE)-NH2==
		+	<StructureSection load='1okw' size='340' side='right' caption='[[1okw]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FCL:3-CHLORO-L-PHENYLALANINE'>FCL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h06\|1h06]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0u\|1h0u]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1oku\|1oku]], [[1okv\|1okv]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pkd\|1pkd]], [[1qmz\|1qmz]], [[1ol1\|1ol1]], [[1ol2\|1ol2]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1okw RCSB], [http://www.ebi.ac.uk/pdbsum/1okw PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/1okw_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Inhibition of CDK2/CA (cyclin-dependent kinase 2/cyclin A complex) activity through blocking of the substrate recognition site in the cyclin A subunit has been demonstrated to be an effective method for inducing apoptosis in tumor cells. We have used the cyclin binding motif (CBM) present in the tumor suppressor proteins p21(WAF1) and p27(KIP1) as a template to optimize the minimal sequence necessary for CDK2/CA inhibition. A series of peptides were prepared, containing nonnatural amino acids, which possess nano- to micromolar CDK2-inhibitory activity. Here we present X-ray structures of the protein complex CDK2/CA, together with the cyclin groove-bound peptides H-Ala-Ala-Abu-Arg-Ser-Leu-Ile-(p-F-Phe)-NH(2) (peptide 1), H-Arg-Arg-Leu-Ile-Phe-NH(2) (peptide 2), Ac-Arg-Arg-Leu-Asn-(m-Cl-Phe)-NH(2) (peptide 3), H-Arg-Arg-Leu-Asn-(p-F-Phe)-NH(2) (peptide 4), and H-Cit-Cit-Leu-Ile-(p-F-Phe)-NH(2) (peptide 5). Some of the peptide complexes presented here were obtained through the novel technique of ligand exchange within protein crystals. This method may find general application for obtaining complex structures of proteins with surface-bound ligands.

-	~~{{STRUCTURE_1okw\| PDB=1okw \| SCENE= }}~~	+	Insights into cyclin groove recognition: complex crystal structures and inhibitor design through ligand exchange.,Kontopidis G, Andrews MJ, McInnes C, Cowan A, Powers H, Innes L, Plater A, Griffiths G, Paterson D, Zheleva DI, Lane DP, Green S, Walkinshaw MD, Fischer PM Structure. 2003 Dec;11(12):1537-46. PMID:14656438<ref>PMID:14656438</ref>

-	~~===CYCLIN A BINDING GROOVE INHIBITOR AC-ARG-ARG-LEU-ASN-(M-CL-PHE)-NH2===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14656438}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1okw]] is~~ a ~~6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA].~~	+

	==See Also==		==See Also==
-	*[[Cell ~~Division Protein Kinase~~ 2\|Cell ~~Division Protein Kinase~~ 2]]	+	*[[Cell division protein kinase 2\|Cell division protein kinase 2]]
	*[[Cyclin\|Cyclin]]		*[[Cyclin\|Cyclin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:014656438<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]

OCA at 09:46, 20 October 2012

OCA — Sat, 20 Oct 2012 09:46:38 GMT

←Older revision		Revision as of 09:46, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1okw]] is a 6 chain structure ~~of [[Cell Division Protein Kinase 2]] and [[Cyclin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA].	+	[[1okw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKW OCA].

	==See Also==		==See Also==