3c3c
From Proteopedia
(Difference between revisions)
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==About this Structure== | ==About this Structure== | ||
- | 3C3C is a | + | 3C3C is a 2 chains structure of sequences 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=3C3C OCA]. |
==Reference== | ==Reference== | ||
- | + | <ref group="xtra">PMID:18463139</ref><references group="xtra"/> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphoglycerate kinase]] | [[Category: Phosphoglycerate kinase]] | ||
- | [[Category: Single protein]] | ||
[[Category: Arold, S T.]] | [[Category: Arold, S T.]] | ||
[[Category: Chaloin, L.]] | [[Category: Chaloin, L.]] | ||
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[[Category: Transferase]] | [[Category: Transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:54:43 2009'' |
Revision as of 10:54, 17 February 2009
Contents |
Crystal Structure of human phosphoglycerate kinase bound to 3-phosphoglycerate and L-CDP
Template:ABSTRACT PUBMED 18463139
Disease
Known disease associated with this structure: Phosphoglycerate kinase 1 deficiency OMIM:[311800]
About this Structure
3C3C is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Gondeau C, Chaloin L, Lallemand P, Roy B, Perigaud C, Barman T, Varga A, Vas M, Lionne C, Arold ST. Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase. Nucleic Acids Res. 2008 Jun;36(11):3620-9. Epub 2008 May 7. PMID:18463139 doi:10.1093/nar/gkn212
Page seeded by OCA on Tue Feb 17 12:54:43 2009
Categories: Homo sapiens | Phosphoglycerate kinase | Arold, S T. | Chaloin, L. | Gondeau, C. | Lionne, C. | Acetylation | Atp-binding | Cytoplasm | Disease mutation | Glycolysis | Hereditary hemolytic anemia | Kinase | L-enantiomer of cdp | Nucleotide-binding | Phosphoprotein | Polymorphism | Protein-nucleotide complex | Transferase