2y3i - Revision history

OCA at 15:45, 4 October 2023

OCA — Wed, 04 Oct 2023 15:45:55 GMT

←Older revision		Revision as of 15:45, 4 October 2023
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	<StructureSection load='2y3i' size='340' side='right'caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2y3i' size='340' side='right'caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3I 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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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]] 2.9Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2x15\|2x15]], [[2wzd\|2wzd]], [[2x13\|2x13]], [[2xe8\|2xe8]]</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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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/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=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [https://pdbe.org/2y3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [https://www.ebi.ac.uk/pdbsum/2y3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3i 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=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [https://pdbe.org/2y3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [https://www.ebi.ac.uk/pdbsum/2y3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3i 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: Bowler MW]]
-	[[Category: Bowler~~, M W~~]]	+	[[Category: Chaloin L]]
-	[[Category: Chaloin, L]]	+	[[Category: Lionne C]]
-	[[Category: Lionne, C]]	+
-	~~[[Category: Aid]]~~	+
-	~~[[Category: Cancer]]~~	+
-	~~[[Category: Glycolysis]]~~	+
-	~~[[Category: Hepatitis]]~~	+
-	~~[[Category: L-nucleoside analogue]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 14:51, 29 December 2021

OCA — Wed, 29 Dec 2021 14:51:18 GMT

OCA at 11:22, 27 March 2020

OCA — Fri, 27 Mar 2020 11:22:38 GMT

←Older revision		Revision as of 11:22, 27 March 2020
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	==The structure of the fully closed conformation of human PGK in complex with L-ADP, 3PG and the TSA aluminium tetrafluoride==		==The structure of the fully closed conformation of human PGK in complex with L-ADP, 3PG and the TSA aluminium tetrafluoride==
-	<StructureSection load='2y3i' size='340' side='right' caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='2y3i' size='340' side='right'caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3I FirstGlance]. <br>		<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3I FirstGlance]. <br>
Line 25:		Line 25:
	==See Also==		==See Also==
	*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]		*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]
		+	*[[Phosphoglycerate kinase 3D structures\|Phosphoglycerate kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
	[[Category: Bowler, M W]]		[[Category: Bowler, M W]]

OCA at 06:04, 20 June 2018

OCA — Wed, 20 Jun 2018 06:04:13 GMT

←Older revision		Revision as of 06:04, 20 June 2018
Line 1:		Line 1:

-	==~~THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN~~ PGK ~~IN COMPLEX WITH~~ L-ADP, 3PG ~~AND THE~~ TSA ~~ALUMINIUM TETRAFLUORIDE~~==	+	==The structure of the fully closed conformation of human PGK in complex with L-ADP, 3PG and the TSA aluminium tetrafluoride==
	<StructureSection load='2y3i' size='340' side='right' caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2y3i' size='340' side='right' caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 10:50, 4 August 2016

OCA — Thu, 04 Aug 2016 10:50:50 GMT

←Older revision		Revision as of 10:50, 4 August 2016
Line 1:		Line 1:
		+
	==THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE==		==THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE==
	<StructureSection load='2y3i' size='340' side='right' caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2y3i' size='340' side='right' caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2y3i]] is a 2 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3I 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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2x15\|2x15]], [[2wzd\|2wzd]], [[2x13\|2x13]], [[2xe8\|2xe8]]</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]], [[2x15\|2x15]], [[2wzd\|2wzd]], [[2x13\|2x13]], [[2xe8\|2xe8]]</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=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [http://www.ebi.ac.uk/pdbsum/2y3i 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=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [http://pdbe.org/2y3i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [http://www.ebi.ac.uk/pdbsum/2y3i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3i 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 2y3i" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
	[[Category: Bowler, M W]]		[[Category: Bowler, M W]]

OCA at 14:25, 18 December 2014

OCA — Thu, 18 Dec 2014 14:25:34 GMT

←Older revision		Revision as of 14:25, 18 December 2014
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-	~~{{STRUCTURE_2y3i\| PDB=2y3i \| SCENE= }}~~	+	==THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE==
-	===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===	+	<StructureSection load='2y3i' size='340' side='right' caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21549713}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2y3i]] is a 2 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3I 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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2x15\|2x15]], [[2wzd\|2wzd]], [[2x13\|2x13]], [[2xe8\|2xe8]]</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=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [http://www.ebi.ac.uk/pdbsum/2y3i 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 ==
		+	Substrate antagonism has been described for a variety of enzymes with more than one substrate and is characterized by a lowering of the affinity of one substrate in the presence of the other(s). 3-Phosphoglycerate kinase (PGK) catalyzes phosphotransfer from 1,3-bisphosphoglycerate (bPG) to ADP to give 3-phosphoglycerate (PG) and ATP, and is subject to substrate antagonism. Because of the instability of bPG, antagonism has only been described between PG and ATP or ADP. Here, we show that antagonism also occurs between bPG and ADP. Using the stopped-flow method, we show that the dissociation constant for one substrate increases in the presence of the other, and that this decrease in affinity is mainly due to an increase in the dissociation rate constant. As a consequence, there is an increase in the overall interaction kinetics. Interestingly, in the presence of the mirror image of natural d-ADP, l-ADP (a good substrate for PGK), antagonism is absent. Using rapid-quench-flow, we studied the kinetics of ATP formation. The time courses present the following: (1) a lag with l-ADP, but not with d-ADP, the kinetics of which were similar to the interaction kinetics measured by stopped-flow; (2) a burst that is directed by the phosphotransfer; and (3) a steady-state that is rate limited by the release of product kinetics. Structural explanations for these results are proposed by analyzing the crystallographic structure of the fully closed conformation of PGK in complex with l-ADP, PG, and the transition-state analogue AlF(4)(-) compared to previously determined structures.

-	~~==Disease==~~	+	Interaction of human 3-phosphoglycerate kinase with its two substrates: is substrate antagonism a kinetic advantage?,Lallemand P, Chaloin L, Roy B, Barman T, Bowler MW, Lionne C J Mol Biol. 2011 Jun 24;409(5):742-57. Epub 2011 Apr 27. PMID:21549713<ref>PMID:21549713</ref>
-	~~[[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==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[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>
-		+
-	~~==About this Structure==~~	+
-	~~[[2y3i]] is a 2 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=2Y3I OCA].~~	+

	==See Also==		==See Also==
	*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]		*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021549713</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
-	[[Category: Bowler, M W.]]	+	[[Category: Bowler, M W]]
-	[[Category: Chaloin, L.]]	+	[[Category: Chaloin, L]]
-	[[Category: Lionne, C.]]	+	[[Category: Lionne, C]]
	[[Category: Aid]]		[[Category: Aid]]
	[[Category: Cancer]]		[[Category: Cancer]]

OCA at 16:56, 24 March 2013

OCA — Sun, 24 Mar 2013 16:56:01 GMT

←Older revision		Revision as of 16:56, 24 March 2013
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-	[[Image:2y3i.png\|left\|200px]]
-
	{{STRUCTURE_2y3i\| PDB=2y3i \| SCENE= }}		{{STRUCTURE_2y3i\| PDB=2y3i \| SCENE= }}
-
	===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===		===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===
		+	{{ABSTRACT_PUBMED_21549713}}

-	~~{{ABSTRACT_PUBMED_21549713}}~~	+	==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).

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021549713</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021549713</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]

OCA at 14:40, 20 October 2012

OCA — Sat, 20 Oct 2012 14:40:26 GMT

←Older revision		Revision as of 14:40, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[2y3i]] is a 2 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=2Y3I OCA].	+	[[2y3i]] is a 2 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=2Y3I OCA].

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

OCA at 15:52, 26 July 2012

OCA — Thu, 26 Jul 2012 15:52:30 GMT

←Older revision		Revision as of 15:52, 26 July 2012
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	[[Image:2y3i.png\|left\|200px]]		[[Image:2y3i.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2y3i\| PDB=2y3i \| SCENE= }}		{{STRUCTURE_2y3i\| PDB=2y3i \| SCENE= }}

	===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===		===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===

-
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	{{ABSTRACT_PUBMED_21549713}}		{{ABSTRACT_PUBMED_21549713}}

	==About this Structure==		==About this Structure==
-	[[2y3i]] is a 2 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=2Y3I OCA].	+	[[2y3i]] is a 2 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=2Y3I OCA].
		+
		+	==See Also==
		+	*[[Phosphoglycerate Kinase\|Phosphoglycerate Kinase]]

	==Reference==		==Reference==

OCA at 05:22, 29 June 2011

OCA — Wed, 29 Jun 2011 05:22:16 GMT

←Older revision		Revision as of 05:22, 29 June 2011
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-	[[Image:2y3i.~~jpg~~\|left\|200px]]	+	[[Image:2y3i.png\|left\|200px]]

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	===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===		===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21549713}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21549713 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21549713}}

	==About this Structure==		==About this Structure==
	[[2y3i]] is a 2 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=2Y3I OCA].		[[2y3i]] is a 2 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=2Y3I OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021549713</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoglycerate kinase]]		[[Category: Phosphoglycerate kinase]]
Line 19:		Line 28:
	[[Category: Chaloin, L.]]		[[Category: Chaloin, L.]]
	[[Category: Lionne, C.]]		[[Category: Lionne, C.]]
		+	[[Category: Aid]]
		+	[[Category: Cancer]]
		+	[[Category: Glycolysis]]
		+	[[Category: Hepatitis]]
		+	[[Category: L-nucleoside analogue]]
		+	[[Category: Transferase]]

←Older revision		Revision as of 14:51, 29 December 2021
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	<StructureSection load='2y3i' size='340' side='right'caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2y3i' size='340' side='right'caption='[[2y3i]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2Y3I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2y3i]] 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=2Y3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3I 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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LA8:L-ADENOSINE-5-DIPHOSPHATE'>LA8</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">[[2xe7\|2xe7]], [[2xe6\|2xe6]], [[2wzb\|2wzb]], [[2wzc\|2wzc]], [[2x14\|2x14]], [[2x15\|2x15]], [[2wzd\|2wzd]], [[2x13\|2x13]], [[2xe8\|2xe8]]</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]], [[2x15\|2x15]], [[2wzd\|2wzd]], [[2x13\|2x13]], [[2xe8\|2xe8]]</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~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [~~http~~://pdbe.org/2y3i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2y3i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3i 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=2y3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3i OCA], [https://pdbe.org/2y3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3i RCSB], [https://www.ebi.ac.uk/pdbsum/2y3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3i 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 ==