2xe8 - Revision history

OCA at 10:29, 20 December 2023

2023-12-20T10:29:42Z

← Older revision		Revision as of 10:29, 20 December 2023
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	<StructureSection load='2xe8' size='340' side='right'caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='2xe8' size='340' side='right'caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=3PG:3~~-~~PHOSPHOGLYCERIC+ACID'>3PG</scene>~~, ~~<scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</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]] 1.79Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3]~~ </~~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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [https://pdbe.org/2xe8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [https://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [https://pdbe.org/2xe8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [https://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[https://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref> <ref>PMID:8043870</ref> <ref>PMID:8615693</ref> <ref>PMID:9744480</ref> <ref>PMID:2001457</ref> <ref>PMID:1586722</ref> <ref>PMID:1547346</ref> <ref>PMID:6941312</ref> <ref>PMID:6933565</ref>		[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[https://omim.org/entry/300653 300653]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref> <ref>PMID:8043870</ref> <ref>PMID:8615693</ref> <ref>PMID:9744480</ref> <ref>PMID:2001457</ref> <ref>PMID:1586722</ref> <ref>PMID:1547346</ref> <ref>PMID:6941312</ref> <ref>PMID:6933565</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).		[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Phosphoglycerate kinase]]~~		[[Category: Baxter NJ]]
	[[Category: Baxter~~, N J~~]]		[[Category: Blackburn GM]]
	[[Category: Blackburn~~, G M~~]]		[[Category: Bowler MW]]
	[[Category: Bowler~~, M W~~]]		[[Category: Cliff MJ]]
	[[Category: Cliff~~, M J~~]]		[[Category: Merli A]]
	[[Category: Merli, A]]		[[Category: Vas M]]
	[[Category: Vas, M]]		[[Category: Waltho JP]]
	[[Category: Waltho~~, J P]]~~
	~~[[Category: Domain motion]]~~
	~~[[Category: Glycolysis]]~~
	~~[[Category: Hereditary hemolytic anemia]]~~
	~~[[Category: Kinase]]~~
	~~[[Category: Nucleotide-binding]]~~
	~~[[Category: Phosphoprotein]]~~
	~~[[Category: Phosphoryl transfer]]~~
	~~[[Category: Transferase]]~~
	~~[[Category: Transition state analogue~~]]

OCA at 10:51, 13 April 2022

2022-04-13T10:51:07Z

OCA at 15:12, 8 July 2020

2020-07-08T15:12:13Z

← Older revision		Revision as of 15:12, 8 July 2020
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	==The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and AMP-PNP==		==The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and AMP-PNP==
	<StructureSection load='2xe8' size='340' side='right' caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='2xe8' size='340' side='right'caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [http://pdbe.org/2xe8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [http://pdbe.org/2xe8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	==See Also==		==See Also==
	*[[Phosphoglycerate ~~Kinase~~\|Phosphoglycerate ~~Kinase~~]]		*[[Phosphoglycerate kinase 3D structures\|Phosphoglycerate kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
	[[Category: Baxter, N J]]		[[Category: Baxter, N J]]

OCA at 09:24, 3 October 2018

2018-10-03T09:24:56Z

← Older revision		Revision as of 09:24, 3 October 2018
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	==~~THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE~~: ~~THE OPEN TERNARY COMPLEX WITH~~ 3PG ~~AND~~ AMP-PNP==		==The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and AMP-PNP==
	<StructureSection load='2xe8' size='340' side='right' caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='2xe8' size='340' side='right' caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 12:15, 5 August 2016

2016-08-05T12:15:02Z

← Older revision		Revision as of 12:15, 5 August 2016
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	==THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP==		==THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP==
	<StructureSection load='2xe8' size='340' side='right' caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='2xe8' size='340' side='right' caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xe8 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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [http://pdbe.org/2xe8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 2xe8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
	[[Category: Baxter, N J]]		[[Category: Baxter, N J]]

OCA at 12:07, 18 December 2014

2014-12-18T12:07:36Z

← Older revision		Revision as of 12:07, 18 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2xe8\| PDB=2xe8 \| SCENE= }}~~		==THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP==
	===THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP===		<StructureSection load='2xe8' size='340' side='right' caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>
	~~{{ABSTRACT_PUBMED_21349853}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>
	==Disease==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>
	[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[http://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref><ref>PMID:8043870</ref><ref>PMID:8615693</ref><ref>PMID:9744480</ref><ref>PMID:2001457</ref><ref>PMID:1586722</ref><ref>PMID:1547346</ref><ref>PMID:6941312</ref><ref>PMID:6933565</ref>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xe8 PDBsum]</span></td></tr>
			</table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[http://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref> <ref>PMID:8043870</ref> <ref>PMID:8615693</ref> <ref>PMID:9744480</ref> <ref>PMID:2001457</ref> <ref>PMID:1586722</ref> <ref>PMID:1547346</ref> <ref>PMID:6941312</ref> <ref>PMID:6933565</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Phosphoglycerate kinase (PGK) is the enzyme responsible for the first ATP-generating step of glycolysis and has been implicated extensively in oncogenesis and its development. Solution small angle x-ray scattering (SAXS) data, in combination with crystal structures of the enzyme in complex with substrate and product analogues, reveal a new conformation for the resting state of the enzyme and demonstrate the role of substrate binding in the preparation of the enzyme for domain closure. Comparison of the x-ray scattering curves of the enzyme in different states with crystal structures has allowed the complete reaction cycle to be resolved both structurally and temporally. The enzyme appears to spend most of its time in a fully open conformation with short periods of closure and catalysis, thereby allowing the rapid diffusion of substrates and products in and out of the binding sites. Analysis of the open apoenzyme structure, defined through deformable elastic network refinement against the SAXS data, suggests that interactions in a mostly buried hydrophobic region may favor the open conformation. This patch is exposed on domain closure, making the open conformation more thermodynamically stable. Ionic interactions act to maintain the closed conformation to allow catalysis. The short time PGK spends in the closed conformation and its strong tendency to rest in an open conformation imply a spring-loaded release mechanism to regulate domain movement, catalysis, and efficient product release.

	~~==Function==~~		A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase.,Zerrad L, Merli A, Schroder GF, Varga A, Graczer E, Pernot P, Round A, Vas M, Bowler MW J Biol Chem. 2011 Apr 22;286(16):14040-8. Epub 2011 Feb 24. PMID:21349853<ref>PMID:21349853</ref>
	~~[[http://www~~.~~uniprot~~.~~org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein~~ (~~primer recognition protein~~).

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[2xe8]] is~~ a ~~1 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=2XE8 OCA].~~		</div>

	==See Also==		==See Also==
	*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]		*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:021349853</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
	[[Category: Baxter, N J.]]		[[Category: Baxter, N J]]
	[[Category: Blackburn, G M.]]		[[Category: Blackburn, G M]]
	[[Category: Bowler, M W.]]		[[Category: Bowler, M W]]
	[[Category: Cliff, M J.]]		[[Category: Cliff, M J]]
	[[Category: Merli, A.]]		[[Category: Merli, A]]
	[[Category: Vas, M.]]		[[Category: Vas, M]]
	[[Category: Waltho, J P.]]		[[Category: Waltho, J P]]
	[[Category: Domain motion]]		[[Category: Domain motion]]
	[[Category: Glycolysis]]		[[Category: Glycolysis]]

OCA at 22:00, 24 March 2013

2013-03-24T22:00:34Z

← Older revision		Revision as of 22:00, 24 March 2013
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	~~[[Image:2xe8.png\|left\|200px]]~~

	{{STRUCTURE_2xe8\| PDB=2xe8 \| SCENE= }}		{{STRUCTURE_2xe8\| PDB=2xe8 \| SCENE= }}
			===THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP===
			{{ABSTRACT_PUBMED_21349853}}

	===~~THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE~~: ~~THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP===~~		==Disease==
			[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[http://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref><ref>PMID:8043870</ref><ref>PMID:8615693</ref><ref>PMID:9744480</ref><ref>PMID:2001457</ref><ref>PMID:1586722</ref><ref>PMID:1547346</ref><ref>PMID:6941312</ref><ref>PMID:6933565</ref>

	~~{{ABSTRACT_PUBMED_21349853}}~~		==Function==
			[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:021349853</ref><references group="xtra"/>		<ref group="xtra">PMID:021349853</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]

OCA at 20:08, 20 October 2012

2012-10-20T20:08:51Z

← Older revision		Revision as of 20:08, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[2xe8]] is a 1 chain structure ~~of [[Phosphoglycerate Kinase]]~~ 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=2XE8 OCA].		[[2xe8]] is a 1 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=2XE8 OCA].

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

OCA at 09:33, 27 July 2012

2012-07-27T09:33:25Z

← Older revision		Revision as of 09:33, 27 July 2012
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	[[Image:2xe8.png\|left\|200px]]		[[Image:2xe8.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2xe8", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2xe8\| PDB=2xe8 \| SCENE= }}		{{STRUCTURE_2xe8\| PDB=2xe8 \| SCENE= }}

	===THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP===		===THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_21349853}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 21349853 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_21349853}}		{{ABSTRACT_PUBMED_21349853}}

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	==See Also==		==See Also==
	*[[Phosphoglycerate Kinase]]		*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]

	==Reference==		==Reference==

OCA at 08:16, 30 October 2011

2011-10-30T08:16:15Z

← Older revision		Revision as of 08:16, 30 October 2011
Line 19:		Line 19:

	==About this Structure==		==About this Structure==
	[[2xe8]] is a 1 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=2XE8 OCA].		[[2xe8]] is a 1 chain structure of [[Phosphoglycerate Kinase]] 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=2XE8 OCA].

			==See Also==
			*[[Phosphoglycerate Kinase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~21349853~~</ref><references group="xtra"/>		<ref group="xtra">PMID:021349853</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
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	[[Category: Vas, M.]]		[[Category: Vas, M.]]
	[[Category: Waltho, J P.]]		[[Category: Waltho, J P.]]
			[[Category: Domain motion]]
			[[Category: Glycolysis]]
			[[Category: Hereditary hemolytic anemia]]
			[[Category: Kinase]]
			[[Category: Nucleotide-binding]]
			[[Category: Phosphoprotein]]
			[[Category: Phosphoryl transfer]]
			[[Category: Transferase]]
			[[Category: Transition state analogue]]

← Older revision		Revision as of 10:51, 13 April 2022
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	<StructureSection load='2xe8' size='340' side='right'caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='2xe8' size='340' side='right'caption='[[2xe8]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xe8]] is a 1 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=2XE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XE8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2wzd\|2wzd]], [[2x15\|2x15]], [[2x13\|2x13]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [~~http~~://pdbe.org/2xe8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 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=2xe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xe8 OCA], [https://pdbe.org/2xe8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xe8 RCSB], [https://www.ebi.ac.uk/pdbsum/2xe8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xe8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[~~http~~://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref> <ref>PMID:8043870</ref> <ref>PMID:8615693</ref> <ref>PMID:9744480</ref> <ref>PMID:2001457</ref> <ref>PMID:1586722</ref> <ref>PMID:1547346</ref> <ref>PMID:6941312</ref> <ref>PMID:6933565</ref>		[[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[https://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref> <ref>PMID:8043870</ref> <ref>PMID:8615693</ref> <ref>PMID:9744480</ref> <ref>PMID:2001457</ref> <ref>PMID:1586722</ref> <ref>PMID:1547346</ref> <ref>PMID:6941312</ref> <ref>PMID:6933565</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).		[[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==