2x15

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{{STRUCTURE_2x15| PDB=2x15 | SCENE= }}
 
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===THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN PHOSPHOGLYCERATE KINASE IN COMPLEX WITH ADP AND 1,3-BISPHOSPHOGLYCERATE===
 
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==Disease==
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==The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3- bisphosphoglycerate==
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[[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>
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<StructureSection load='2x15' size='340' side='right'caption='[[2x15]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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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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[[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).
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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='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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==About this Structure==
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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>
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[[2x15]] 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=2X15 OCA].
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</table>
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== 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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== 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).
==See Also==
==See Also==
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*[[Phosphoglycerate Kinase|Phosphoglycerate Kinase]]
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*[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Phosphoglycerate kinase]]
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[[Category: Large Structures]]
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[[Category: Baxter, N J.]]
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[[Category: Baxter NJ]]
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[[Category: Blackburn, G M.]]
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[[Category: Blackburn GM]]
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[[Category: Bowler, M W.]]
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[[Category: Bowler MW]]
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[[Category: Cliff, M J.]]
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[[Category: Cliff MJ]]
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[[Category: Hounslow, A M.H.]]
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[[Category: Hounslow AMH]]
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[[Category: Marston, J P.M.]]
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[[Category: Marston JPM]]
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[[Category: Szabo, J.]]
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[[Category: Szabo J]]
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[[Category: Varga, A V.]]
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[[Category: Varga AV]]
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[[Category: Vas, M.]]
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[[Category: Vas M]]
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[[Category: Waltho, J P.]]
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[[Category: Waltho JP]]
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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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