2vgf: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2VGF is a | 2VGF 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=1liw 1liw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGF 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: Abraham, D J.]] | [[Category: Abraham, D J.]] | ||
[[Category: Bianchi, P.]] | [[Category: Bianchi, P.]] | ||
Line 49: | Line 48: | ||
[[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 Mon Feb 16 12:59:36 2009'' |
Revision as of 13:59, 16 February 2009
HUMAN ERYTHROCYTE PYRUVATE KINASE: T384M MUTANTHUMAN ERYTHROCYTE PYRUVATE KINASE: T384M MUTANT
Template:ABSTRACT PUBMED 11960989
About this StructureAbout this Structure
2VGF is a 4 chains structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1liw. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
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OCACategories:
- Pages with broken file links
- 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