2vgg
From Proteopedia
(Difference between revisions)
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==About this Structure== | ==About this Structure== | ||
- | 2VGG is a | + | 2VGG is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liy 1liy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGG OCA]. |
==Reference== | ==Reference== | ||
- | + | <ref group="xtra">PMID:11960989</ref><references group="xtra"/> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Pyruvate kinase]] | [[Category: Pyruvate kinase]] | ||
- | [[Category: Single protein]] | ||
[[Category: Abraham, D J.]] | [[Category: Abraham, D J.]] | ||
[[Category: Bianchi, P.]] | [[Category: Bianchi, P.]] | ||
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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 16:16:00 2009'' |
Revision as of 14:16, 17 February 2009
HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT
Template:ABSTRACT PUBMED 11960989
About this Structure
2VGG is a 4 chains structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1liy. Full crystallographic information is available from OCA.
Reference
- Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A. Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. PMID:11960989 doi:10.1074/jbc.M202107200
Page seeded by OCA on Tue Feb 17 16:16:00 2009
Categories: Homo sapiens | Pyruvate kinase | Abraham, D J. | Bianchi, P. | Chiarelli, L. | Dolzan, M. | Fortin, R. | Galizzi, A. | Mattevi, A. | Valentini, G. | Wang, C. | Zanella, A. | Alternative splicing | Disease mutation | Glycolysis | Kinase | Magnesium | Metal-binding | Phosphorylation | Polymorphism | Pyruvate | Pyruvate kinase in the active r-state | Transferase