This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2v0l
From Proteopedia
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 Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU)., Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L, Protein Sci. 2007 Dec;16(12):2657-66. PMID:18029420
Page seeded by OCA on Mon Jul 28 16:52:13 2008
Categories: Haemophilus influenzae | Single protein | 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
