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2v0l
From Proteopedia
m (Protected "2v0l" [edit=sysop:move=sysop]) |
Revision as of 20:49, 7 January 2013
CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS OF THE POTENTIAL ANTIBACTERIAL TARGET N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE (GLMU)
Template:ABSTRACT PUBMED 18029420
About this Structure
2v0l is a 1 chain structure with sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
- Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L. Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 2007 Dec;16(12):2657-66. PMID:18029420 doi:http://dx.doi.org/16/12/2657
Categories: Haemophilus influenzae | Chirgadze, N Y. | Lightle, S. | Mochalkin, I. | Ohren, J F. | Acyltransferase | Associative mechanism | Catalytic mechanism | Cell shape | Cell wall | Glmu | Magnesium | Metal-binding | Multifunctional enzyme | Nucleotidyltransferase | Peptidoglycan synthesis | Transferase | Uridylation
