2x15: Difference between revisions

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-'''Unreleased structure'''
-The entry 2x15 is ON HOLD
+==The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3- bisphosphoglycerate==
+<StructureSection load='2x15' size='340' side='right'caption='[[2x15]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+== 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>
+== 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).
-Authors: Bowler, M.W., Cliff, M.J., Marston, J.P.M., Baxter, N.J., Hownslow, A.M.H., Varga, A.V., Szabo, J., Vas, M., Blackburn, G.M., Waltho, J.P.
+==See Also==
+*[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]]
-Description: The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3-bisphosphoglycerate
+== References ==
+<references/>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:28:34 2010''
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Baxter NJ]]
+[[Category: Blackburn GM]]
+[[Category: Bowler MW]]
+[[Category: Cliff MJ]]
+[[Category: Hounslow AMH]]
+[[Category: Marston JPM]]
+[[Category: Szabo J]]
+[[Category: Varga AV]]
+[[Category: Vas M]]
+[[Category: Waltho JP]]