4bbq - Revision history

OCA at 10:59, 9 May 2024

OCA — Thu, 09 May 2024 10:59:05 GMT

←Older revision		Revision as of 10:59, 9 May 2024
Line 3:		Line 3:
	<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bbq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1~~,2~~-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.24Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https:~~/~~/en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase]~~, ~~with EC number [https~~:~~//www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [https://pdbe.org/4bbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [https://www.ebi.ac.uk/pdbsum/4bbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbq 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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [https://pdbe.org/4bbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [https://www.ebi.ac.uk/pdbsum/4bbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>	+	[https://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>

	==See Also==		==See Also==
Line 17:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Allerston~~, C K~~]]	+	[[Category: Allerston CK]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: Ball, L]]	+	[[Category: Ball L]]
-	[[Category: Bountra, C]]	+	[[Category: Bountra C]]
-	[[Category: Chen, Y]]	+	[[Category: Chen Y]]
-	~~[[Category: Delft, F von~~]]	+	[[Category: Edlich C]]
-	[[Category: Edlich, C]]	+	[[Category: Edwards A]]
-	[[Category: Edwards, A]]	+	[[Category: Gileadi O]]
-	[[Category: Gileadi, O]]	+	[[Category: Krojer T]]
-	[[Category: Krojer, T]]	+	[[Category: Laue ED]]
-	[[Category: Laue~~, E D~~]]	+	[[Category: Li B]]
-	[[Category: Li, B]]	+	[[Category: Watson AA]]
-	[[Category: Watson~~, A A~~]]	+	[[Category: Von Delft F]]
-	[[Category: ~~Chromatin]]~~	+
-	~~[[Category: Cpg island]]~~	+
-	~~[[Category: Demethylation]]~~	+
-	~~[[Category: Fbxl11]]~~	+
-	~~[[Category: Kdm2a]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Ubiquitin]]~~	+
-	~~[[Category: Ubiquitination]]~~	+
-	~~[[Category: Zf-cxxc dna binding domain~~]]	+

OCA at 07:07, 31 August 2022

OCA — Wed, 31 Aug 2022 07:07:04 GMT

←Older revision		Revision as of 07:07, 31 August 2022
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	<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [~~http~~://pdbe.org/4bbq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4bbq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbq 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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [https://pdbe.org/4bbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [https://www.ebi.ac.uk/pdbsum/4bbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>	+	[[https://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>

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

OCA at 16:35, 29 January 2020

OCA — Wed, 29 Jan 2020 16:35:48 GMT

←Older revision		Revision as of 16:35, 29 January 2020
Line 1:		Line 1:

	==Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)==		==Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)==
-	<StructureSection load='4bbq' size='340' side='right' caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>	+	<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>		[[http://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>
		+
		+	==See Also==
		+	*[[Lysine-specific histone demethylase 3D structures\|Lysine-specific histone demethylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 15:		Line 18:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Allerston, C K]]		[[Category: Allerston, C K]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]

OCA at 19:46, 24 January 2018

OCA — Wed, 24 Jan 2018 19:46:54 GMT

←Older revision		Revision as of 19:46, 24 January 2018
Line 20:		Line 20:
	[[Category: Bountra, C]]		[[Category: Bountra, C]]
	[[Category: Chen, Y]]		[[Category: Chen, Y]]
-	[[Category: Delft, F ~~Von~~]]	+	[[Category: Delft, F von]]
	[[Category: Edlich, C]]		[[Category: Edlich, C]]
	[[Category: Edwards, A]]		[[Category: Edwards, A]]

OCA at 13:22, 4 August 2016

OCA — Thu, 04 Aug 2016 13:22:45 GMT

←Older revision		Revision as of 13:22, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)==		==Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)==
	<StructureSection load='4bbq' size='340' side='right' caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='4bbq' size='340' side='right' caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [http://www.ebi.ac.uk/pdbsum/4bbq 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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [http://pdbe.org/4bbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [http://www.ebi.ac.uk/pdbsum/4bbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 09:41, 25 December 2014

OCA — Thu, 25 Dec 2014 09:41:19 GMT

←Older revision		Revision as of 09:41, 25 December 2014
Line 1:		Line 1:
-	~~[[Image:4bbq.jpg\|left\|200px]]~~	+	==Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)==
-		+	<StructureSection load='4bbq' size='340' side='right' caption='[[4bbq]], [[Resolution\|resolution]] 2.24Å' scene=''>
-	~~{{STRUCTURE_4bbq\| PDB=4bbq \| SCENE= }}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BBQ FirstGlance]. <br>
-	===Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)===	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Histone_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [http://www.ebi.ac.uk/pdbsum/4bbq PDBsum]</span></td></tr>
-	==~~About this Structure~~==	+	</table>
-	[[4bbq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBQ OCA].	+	== Function ==
-	[[Category: Allerston, C K.]]	+	[[http://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref>
-	[[Category: Arrowsmith, C H.]]	+	== References ==
-	[[Category: Ball, L.]]	+	<references/>
-	[[Category: Bountra, C.]]	+	__TOC__
-	[[Category: Chen, Y.]]	+	</StructureSection>
-	[[Category: Delft, F Von.]]	+	[[Category: Human]]
-	[[Category: Edlich, C.]]	+	[[Category: Allerston, C K]]
-	[[Category: Edwards, A.]]	+	[[Category: Arrowsmith, C H]]
-	[[Category: Gileadi, O.]]	+	[[Category: Ball, L]]
-	[[Category: Krojer, T.]]	+	[[Category: Bountra, C]]
-	[[Category: Laue, E D.]]	+	[[Category: Chen, Y]]
-	[[Category: Li, B.]]	+	[[Category: Delft, F Von]]
-	[[Category: Watson, A A.]]	+	[[Category: Edlich, C]]
		+	[[Category: Edwards, A]]
		+	[[Category: Gileadi, O]]
		+	[[Category: Krojer, T]]
		+	[[Category: Laue, E D]]
		+	[[Category: Li, B]]
		+	[[Category: Watson, A A]]
	[[Category: Chromatin]]		[[Category: Chromatin]]
	[[Category: Cpg island]]		[[Category: Cpg island]]

OCA at 07:26, 10 October 2012

OCA — Wed, 10 Oct 2012 07:26:27 GMT

←Older revision		Revision as of 07:26, 10 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4bbq.jpg\|left\|200px]]

-	~~The entry~~ 4bbq ~~is ON HOLD~~	+	{{STRUCTURE_4bbq\| PDB=4bbq \| SCENE= }}

-	~~Authors: Allerston, C.K., Watson, A.A., Edlich, C., Li, B., Chen, Y., Ball, L., Krojer, T., Arrowsmith, C.H., Edwards, A., Bountra, C., vonDelft, F., Laue, E.D., Gileadi, O.~~	+	===Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)===

-	~~Description: Crystal~~ structure ~~of the CXXC and PHD domain of Human Lysine~~-~~specific Demethylase 2A (KDM2A)(FBXL11)~~	+
		+	==About this Structure==
		+	[[4bbq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBQ OCA].
		+	[[Category: Allerston, C K.]]
		+	[[Category: Arrowsmith, C H.]]
		+	[[Category: Ball, L.]]
		+	[[Category: Bountra, C.]]
		+	[[Category: Chen, Y.]]
		+	[[Category: Delft, F Von.]]
		+	[[Category: Edlich, C.]]
		+	[[Category: Edwards, A.]]
		+	[[Category: Gileadi, O.]]
		+	[[Category: Krojer, T.]]
		+	[[Category: Laue, E D.]]
		+	[[Category: Li, B.]]
		+	[[Category: Watson, A A.]]
		+	[[Category: Chromatin]]
		+	[[Category: Cpg island]]
		+	[[Category: Demethylation]]
		+	[[Category: Fbxl11]]
		+	[[Category: Kdm2a]]
		+	[[Category: Ligase]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Ubiquitin]]
		+	[[Category: Ubiquitination]]
		+	[[Category: Zf-cxxc dna binding domain]]

OCA: Protected "4bbq" [edit=sysop:move=sysop]

OCA — Wed, 03 Oct 2012 05:36:44 GMT

Protected "4bbq" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:36, 3 October 2012

OCA: New page: '''Unreleased structure''' The entry 4bbq is ON HOLD Authors: Allerston, C.K., Watson, A.A., Edlich, C., Li, B., Chen, Y., Ball, L., Krojer, T., Arrowsmith, C.H., Edwards, A., Bountra, ...

OCA — Wed, 03 Oct 2012 05:36:43 GMT

New page: '''Unreleased structure''' The entry 4bbq is ON HOLD Authors: Allerston, C.K., Watson, A.A., Edlich, C., Li, B., Chen, Y., Ball, L., Krojer, T., Arrowsmith, C.H., Edwards, A., Bountra, ...

New page

'''Unreleased structure'''

The entry 4bbq is ON HOLD

Authors: Allerston, C.K., Watson, A.A., Edlich, C., Li, B., Chen, Y., Ball, L., Krojer, T., Arrowsmith, C.H., Edwards, A., Bountra, C., vonDelft, F., Laue, E.D., Gileadi, O.

Description: Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)