2x15

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Current revision (10:21, 20 December 2023) (edit) (undo)
 
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<StructureSection load='2x15' size='340' side='right'caption='[[2x15]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2x15' size='340' side='right'caption='[[2x15]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2x15]] 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=2X15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X15 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2x15]] 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=2X15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X15 FirstGlance]. <br>
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</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=X15:1,3-BISPHOSPHOGLYCERIC+ACID'>X15</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xe7|2xe7]], [[2y3i|2y3i]], [[2xe6|2xe6]], [[2wzb|2wzb]], [[2wzc|2wzc]], [[2x14|2x14]], [[2wzd|2wzd]], [[2x13|2x13]], [[2xe8|2xe8]]</div></td></tr>
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<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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=X15:1,3-BISPHOSPHOGLYCERIC+ACID'>X15</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x15 OCA], [https://pdbe.org/2x15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x15 RCSB], [https://www.ebi.ac.uk/pdbsum/2x15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x15 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=2x15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x15 OCA], [https://pdbe.org/2x15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x15 RCSB], [https://www.ebi.ac.uk/pdbsum/2x15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x15 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[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>
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[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 ==
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[[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).
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[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).
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phosphoglycerate kinase]]
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[[Category: Baxter NJ]]
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[[Category: Baxter, N J]]
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[[Category: Blackburn GM]]
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[[Category: Blackburn, G M]]
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[[Category: Bowler MW]]
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[[Category: Bowler, M W]]
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[[Category: Cliff MJ]]
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[[Category: Cliff, M J]]
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[[Category: Hounslow AMH]]
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[[Category: Hounslow, A M.H]]
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[[Category: Marston JPM]]
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[[Category: Marston, J P.M]]
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[[Category: Szabo J]]
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[[Category: Szabo, J]]
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[[Category: Varga AV]]
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[[Category: Varga, A V]]
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[[Category: Vas M]]
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[[Category: Vas, M]]
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[[Category: Waltho JP]]
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[[Category: Waltho, J P]]
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[[Category: Glycolysis]]
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[[Category: Hereditary hemolytic anemia]]
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[[Category: Kinase]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Phosphoryl transfer]]
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[[Category: Transferase]]
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[[Category: Transition state analogue]]
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Current revision

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3- bisphosphoglycerate

PDB ID 2x15

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OCA

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