5m6z
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | The | + | ==The X-ray structure of human M189I PGK-1 mutant in partially closed conformation== |
- | + | <StructureSection load='5m6z' size='340' side='right' caption='[[5m6z]], [[Resolution|resolution]] 1.67Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5m6z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M6Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M6Z 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
- | [[Category: | + | <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=5m6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m6z OCA], [http://pdbe.org/5m6z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m6z RCSB], [http://www.ebi.ac.uk/pdbsum/5m6z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m6z ProSAT]</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). | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Phosphoglycerate kinase]] | ||
[[Category: Cipollone, A]] | [[Category: Cipollone, A]] | ||
[[Category: Fiorillo, A]] | [[Category: Fiorillo, A]] | ||
+ | [[Category: Ilari, A]] | ||
[[Category: Petrosino, M]] | [[Category: Petrosino, M]] | ||
- | [[Category: | + | [[Category: Human phosphoglycerate kinase 1]] |
+ | [[Category: M189i snp -derived mutant]] | ||
+ | [[Category: Transferase]] |
Revision as of 06:06, 29 November 2017
The X-ray structure of human M189I PGK-1 mutant in partially closed conformation
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