1h74 - Revision history

OCA at 12:19, 13 December 2023

2023-12-13T12:19:20Z

←Older revision		Revision as of 12:19, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1h74' size='340' side='right'caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1h74' size='340' side='right'caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_43067 Atcc 43067~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H74 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H74 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.9Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [https://pdbe.org/1h74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [https://www.ebi.ac.uk/pdbsum/1h74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h74 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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [https://pdbe.org/1h74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [https://www.ebi.ac.uk/pdbsum/1h74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h74 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA]] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).	+	[https://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 43067]]
-	[[Category: Homoserine kinase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Daugherty, M]]	+	[[Category: Methanocaldococcus jannaschii]]
-	[[Category: Krishna~~, S S~~]]	+	[[Category: Daugherty M]]
-	[[Category: Osterman~~, A L~~]]	+	[[Category: Krishna SS]]
-	[[Category: Zhang, H]]	+	[[Category: Osterman AL]]
-	[[Category: Zhou, T]]	+	[[Category: Zhang H]]
-	~~[[Category: Kinase]]~~	+	[[Category: Zhou T]]
-	~~[[Category: Transferase~~]]	+

OCA at 07:05, 24 February 2021

2021-02-24T07:05:48Z

←Older revision		Revision as of 07:05, 24 February 2021
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	<StructureSection load='1h74' size='340' side='right'caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1h74' size='340' side='right'caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1H74 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H74 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [~~http~~://pdbe.org/1h74 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1h74 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1h74 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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [https://pdbe.org/1h74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [https://www.ebi.ac.uk/pdbsum/1h74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h74 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA]] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).	+	[[https://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA]] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:03, 23 May 2019

2019-05-23T07:03:21Z

←Older revision		Revision as of 07:03, 23 May 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE==		==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE==
-	<StructureSection load='1h74' size='340' side='right' caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1h74' size='340' side='right'caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>
Line 36:		Line 36:
	[[Category: Atcc 43067]]		[[Category: Atcc 43067]]
	[[Category: Homoserine kinase]]		[[Category: Homoserine kinase]]
		+	[[Category: Large Structures]]
	[[Category: Daugherty, M]]		[[Category: Daugherty, M]]
	[[Category: Krishna, S S]]		[[Category: Krishna, S S]]

OCA at 09:23, 10 January 2018

2018-01-10T09:23:44Z

←Older revision		Revision as of 09:23, 10 January 2018
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE==		==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE==
	<StructureSection load='1h74' size='340' side='right' caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1h74' size='340' side='right' caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://pdbe.org/1h74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://pdbe.org/1h74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h74 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/1h74_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/1h74_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>

OCA at 15:29, 9 February 2016

2016-02-09T15:29:51Z

←Older revision		Revision as of 15:29, 9 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=1h74 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 23:36, 10 September 2015

2015-09-10T23:36:01Z

←Older revision		Revision as of 23:36, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1h74' size='340' side='right' caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1h74' size='340' side='right' caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Methanocaldococcus_jannaschii Methanocaldococcus jannaschii~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://pdbe.org/1h74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 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 1h74" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 43067]]
	[[Category: Homoserine kinase]]		[[Category: Homoserine kinase]]
-	[[Category: Methanocaldococcus jannaschii]]
	[[Category: Daugherty, M]]		[[Category: Daugherty, M]]
	[[Category: Krishna, S S]]		[[Category: Krishna, S S]]

OCA at 07:44, 25 December 2014

2014-12-25T07:44:25Z

←Older revision		Revision as of 07:44, 25 December 2014
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	<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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA]] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 19:44, 22 December 2014

2014-12-22T19:44:09Z

←Older revision		Revision as of 19:44, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	[[Category: Homoserine kinase]]		[[Category: Homoserine kinase]]
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]
-	[[Category: Daugherty, M.]]	+	[[Category: Daugherty, M]]
-	[[Category: Krishna, S S.]]	+	[[Category: Krishna, S S]]
-	[[Category: Osterman, A L.]]	+	[[Category: Osterman, A L]]
-	[[Category: Zhang, H.]]	+	[[Category: Zhang, H]]
-	[[Category: Zhou, T.]]	+	[[Category: Zhou, T]]
	[[Category: Kinase]]		[[Category: Kinase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 14:42, 29 September 2014

2014-09-29T14:42:22Z

←Older revision		Revision as of 14:42, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1h74.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE==
		+	<StructureSection load='1h74' size='340' side='right' caption='[[1h74]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1h74]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H74 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fwk\|1fwk]], [[1fwl\|1fwl]], [[1h72\|1h72]], [[1h73\|1h73]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1h74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h74 RCSB], [http://www.ebi.ac.uk/pdbsum/1h74 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/h7/1h74_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 ==
		+	Homoserine kinase (HSK), the fourth enzyme in the aspartate pathway of amino acid biosynthesis, catalyzes the phosphorylation of L-homoserine (Hse) to L-homoserine phosphate, an intermediate in the production of L-threonine, L-isoleucine, and in higher plants, L-methionine. The high-resolution structures of Methanococcus jannaschii HSK ternary complexes with its amino acid substrate and ATP analogues have been determined by X-ray crystallography. These structures reveal the structural determinants of the tight and highly specific binding of Hse, which is coupled with local conformational changes that enforce the sequestration of the substrate. The delta-hydroxyl group of bound Hse is only 3.4 A away from the gamma-phosphate of the bound nucleotide, poised for the in-line attack at the gamma-phosphorus. The bound nucleotides are flexible at the triphosphate tail. Nevertheless, a Mg(2+) was located in one of the complexes that binds between the beta- and gamma-phosphates of the nucleotide with good ligand geometry and is coordinated by the side chain of Glu130. No strong nucleophile (base) can be located near the phosphoryl acceptor hydroxyl group. Therefore, we propose that the catalytic mechanism of HSK does not involve a catalytic base for activating the phosphoryl acceptor hydroxyl but instead is mediated via a transition state stabilization mechanism.

-	~~{{STRUCTURE_1h74\| PDB=1h74 \| SCENE= }}~~	+	Structural basis for the catalysis and substrate specificity of homoserine kinase.,Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:11535056<ref>PMID:11535056</ref>

-	~~===CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11535056}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1h74]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1H74 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011535056<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homoserine kinase]]		[[Category: Homoserine kinase]]
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]

OCA at 09:34, 16 January 2013

2013-01-16T09:34:55Z

←Older revision		Revision as of 09:34, 16 January 2013
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	[[Image:1h74.png\|left\|200px]]		[[Image:1h74.png\|left\|200px]]

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	{{STRUCTURE_1h74\| PDB=1h74 \| SCENE= }}		{{STRUCTURE_1h74\| PDB=1h74 \| SCENE= }}

	===CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE===		===CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE===

-
-	<!--
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	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11535056</ref><ref group="xtra">PMID:11188689~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011535056</ref><references group="xtra"/>
	[[Category: Homoserine kinase]]		[[Category: Homoserine kinase]]
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]