4v7n - Revision history

OCA at 18:04, 20 September 2023

OCA — Wed, 20 Sep 2023 18:04:22 GMT

←Older revision		Revision as of 18:04, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Namalycastis_sp._ST01 Namalycastis sp. ST01]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V7N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Namalycastis_sp._ST01 Namalycastis sp. ST01]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V7N 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 2.3Å</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [https://pdbe.org/4v7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [https://www.ebi.ac.uk/pdbsum/4v7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7n 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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [https://pdbe.org/4v7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [https://www.ebi.ac.uk/pdbsum/4v7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7n ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:11, 29 March 2023

OCA — Wed, 29 Mar 2023 08:11:25 GMT

←Older revision		Revision as of 08:11, 29 March 2023
Line 1:		Line 1:
-	~~{{Large structure}}~~	+
	==Glycocyamine kinase, beta-beta homodimer from marine worm Namalycastis sp., with transition state analog Mg(II)-ADP-NO3-glycocyamine.==		==Glycocyamine kinase, beta-beta homodimer from marine worm Namalycastis sp., with transition state analog Mg(II)-ADP-NO3-glycocyamine.==
-	<StructureSection load='4v7n' size='340' side='right' caption='[[4v7n]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4v7n' size='340' side='right'caption='[[4v7n]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Namalycastis_sp.~~_st01~~ Namalycastis sp. ~~st01~~]. This structure supersedes ~~and combines~~ the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4V7N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Namalycastis_sp._ST01 Namalycastis sp. ST01]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V7N 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l2d\|3l2d]], [[3l2e\|3l2e]]</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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [https://pdbe.org/4v7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [https://www.ebi.ac.uk/pdbsum/4v7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7n ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GK-beta, GK_beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243920 Namalycastis sp. ST01])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanidinoacetate_kinase Guanidinoacetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.1 2.7.3.1] </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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [~~http~~://pdbe.org/4v7n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4v7n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7n ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~{{Large structure}}~~	+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q6AW42_9ANNE Q6AW42_9ANNE]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Guanidinoacetate kinase~~]]	+	[[Category: Large Structures]]
-	[[Category: Namalycastis sp. ~~st01~~]]	+	[[Category: Namalycastis sp. ST01]]
-	[[Category: Herzberg, O]]	+	[[Category: Herzberg O]]
-	[[Category: Lim, K]]	+	[[Category: Lim K]]
-	[[Category: Pullalarevu, S]]	+	[[Category: Pullalarevu S]]
-	~~[[Category: Glycocyamine kinase]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Phosphagen kinase]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transition state analog~~]]	+

OCA at 10:39, 22 November 2017

OCA — Wed, 22 Nov 2017 10:39:37 GMT

←Older revision		Revision as of 10:39, 22 November 2017
Line 1:		Line 1:
		+	{{Large structure}}
	==Glycocyamine kinase, beta-beta homodimer from marine worm Namalycastis sp., with transition state analog Mg(II)-ADP-NO3-glycocyamine.==		==Glycocyamine kinase, beta-beta homodimer from marine worm Namalycastis sp., with transition state analog Mg(II)-ADP-NO3-glycocyamine.==
	<StructureSection load='4v7n' size='340' side='right' caption='[[4v7n]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4v7n' size='340' side='right' caption='[[4v7n]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V7N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure with sequence from [http://en.wikipedia.org/wiki/Namalycastis_sp._st01 Namalycastis sp. st01]. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V7N 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l2d\|3l2d]], [[3l2e\|3l2e]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l2d\|3l2d]], [[3l2e\|3l2e]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GK-beta, GK_beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243920 Namalycastis sp. ST01])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanidinoacetate_kinase Guanidinoacetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.1 2.7.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanidinoacetate_kinase Guanidinoacetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.1 2.7.3.1] </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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [http://www.ebi.ac.uk/pdbsum/4v7n 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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [http://pdbe.org/4v7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [http://www.ebi.ac.uk/pdbsum/4v7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7n ProSAT]</span></td></tr>
	</table>		</table>
	{{Large structure}}		{{Large structure}}
Line 17:		Line 19:
	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 4v7n" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 22:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Guanidinoacetate kinase]]		[[Category: Guanidinoacetate kinase]]
		+	[[Category: Namalycastis sp. st01]]
	[[Category: Herzberg, O]]		[[Category: Herzberg, O]]
	[[Category: Lim, K]]		[[Category: Lim, K]]

OCA at 16:07, 1 September 2015

OCA — Tue, 01 Sep 2015 16:07:36 GMT

←Older revision		Revision as of 16:07, 1 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V7N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V7N 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">~~[[3l2f\|3l2f]], [[3l2g\|3l2g]],~~ [[3l2d\|3l2d]], [[3l2e\|3l2e]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l2d\|3l2d]], [[3l2e\|3l2e]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanidinoacetate_kinase Guanidinoacetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.1 2.7.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanidinoacetate_kinase Guanidinoacetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.1 2.7.3.1] </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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [http://www.ebi.ac.uk/pdbsum/4v7n 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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [http://www.ebi.ac.uk/pdbsum/4v7n PDBsum]</span></td></tr>

OCA: Protected "4v7n" [edit=sysop:move=sysop]

OCA — Tue, 01 Sep 2015 13:13:52 GMT

Protected "4v7n" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:13, 1 September 2015

OCA: New page: ==Glycocyamine kinase, beta-beta homodimer from marine worm Namalycastis sp., with transition state analog Mg(II)-ADP-NO3-glycocyamine.== == Structural highlights ==
<table><tr><td colspan='2'>[[4v7n]] is a 36 chain structure. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2f 3l2f] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l2g 3l2g]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V7N 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMG:GUANIDINO+ACETATE'>NMG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l2f|3l2f]], [[3l2g|3l2g]], [[3l2d|3l2d]], [[3l2e|3l2e]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanidinoacetate_kinase Guanidinoacetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.1 2.7.3.1] </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=4v7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v7n RCSB], [http://www.ebi.ac.uk/pdbsum/4v7n PDBsum]</span></td></tr>
</table>
{{Large structure}}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycocyamine kinase (GK), a member of the phosphagen kinase family, catalyzes the Mg(2+)-dependent reversible phosphoryl group transfer of the N-phosphoryl group of phosphoglycocyamine to ADP to yield glycocyamine and ATP. This reaction helps to maintain the energy homeostasis of the cell in some multicelullar organisms that encounter high and variable energy turnover. GK from the marine worm Namalycastis sp. is heterodimeric, with two homologous polypeptide chains, alpha and beta, derived from a common pre-mRNA by mutually exclusive N-terminal alternative exons. The N-terminal exon of GKbeta encodes a peptide that is different in sequence and is 16 amino acids longer than that encoded by the N-terminal exon of GKalpha. The crystal structures of recombinant GKalphabeta and GKbetabeta from Namalycastis sp. were determined at 2.6 and 2.4 A resolution, respectively. In addition, the structure of the GKbetabeta was determined at 2.3 A resolution in complex with a transition state analogue, Mg(2+)-ADP-NO(3)(-)-glycocyamine. Consistent with the sequence homology, the GK subunits adopt the same overall fold as that of other phosphagen kinases of known structure (the homodimeric creatine kinase (CK) and the monomeric arginine kinase (AK)). As with CK, the GK N-termini mediate the dimer interface. In both heterodimeric and homodimeric GK forms, the conformations of the two N-termini are asymmetric, and the asymmetry is different than that reported previously for the homodimeric CKs from several organisms. The entire polypeptide chains of GKalphabeta are structurally defined, and the longer N-terminus of the beta subunit is anchored at the dimer interface. In GKbetabeta the 24 N-terminal residues of one subunit and 11 N-terminal residues of the second subunit are disordered. This observation is consistent with a proposal that the GKalphabeta amino acids involved in the interface formation were optimized once a heterodimer emerged as the physiological form of the enzyme. As a consequence, the homodimer interface (either solely alpha or solely beta chains) has been corrupted. In the unbound state, GK exhibits an open conformation analogous to that observed with ligand-free CK or AK. Upon binding the transition state analogue, both subunits of GK undergo the same closure motion that clasps the transition state analogue, in contrast to the transition state analogue complexes of CK, where the corresponding transition state analogue occupies only one subunit, which undergoes domain closure. The active site environments of the GK, CK, and AK at the bound states reveal the structural determinants of substrate specificity. Despite the equivalent binding in both active sites of the GK dimer, the conformational asymmetry of the N-termini is retained. Thus, the coupling between the structural asymmetry and negative cooperativity previously proposed for CK is not supported in the case of GK.

Structural basis for the mechanism and substrate specificity of glycocyamine kinase, a phosphagen kinase family member (,).,Lim K, Pullalarevu S, Surabian KT, Howard A, Suzuki T, Moult J, Herzberg O Biochemistry. 2010 Mar 9;49(9):2031-41. PMID:20121101<ref>PMID:20121101</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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TOC
</StructureSection>
[[Category: Guanidinoacetate kinase]]
[[Category: Herzberg, O]]
[[Category: Lim, K]]
[[Category: Pullalarevu, S]]
[[Category: Glycocyamine kinase]]
[[Category: Kinase]]
[[Category: Phosphagen kinase]]
[[Category: Transferase]]
[[Category: Transition state analog]]