5m6z

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'''Unreleased structure'''
 
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The entry 5m6z is ON HOLD
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==The X-ray structure of human M189I PGK-1 mutant in partially closed conformation==
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<StructureSection load='5m6z' size='340' side='right' caption='[[5m6z]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
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Authors: Ilari, A., Fiorillo, A., Petrosino, M., Cipollone, A.
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== Structural highlights ==
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<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>
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Description: The X-ray structure of human M189I PGK-1 mutant in partially closed conformation
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</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>
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[[Category: Unreleased Structures]]
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<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>
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<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>
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</table>
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== Disease ==
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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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== Function ==
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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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Phosphoglycerate kinase]]
[[Category: Cipollone, A]]
[[Category: Cipollone, A]]
[[Category: Fiorillo, A]]
[[Category: Fiorillo, A]]
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[[Category: Ilari, A]]
[[Category: Petrosino, M]]
[[Category: Petrosino, M]]
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[[Category: Ilari, A]]
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[[Category: Human phosphoglycerate kinase 1]]
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[[Category: M189i snp -derived mutant]]
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[[Category: Transferase]]

Revision as of 06:06, 29 November 2017

The X-ray structure of human M189I PGK-1 mutant in partially closed conformation

5m6z, resolution 1.67Å

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