2V0K

Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)

Summary for 2V0K

• Entry DOI: 10.2210/pdb2v0k/pdb
• Related: 2V0H 2V0I 2V0J 2V0L
• Descriptor: BIFUNCTIONAL PROTEIN GLMU, URIDINE-5'-DIPHOSPHATE, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: glmu, cell wall, magnesium, cell shape, transferase, peptidoglycan synthesis, associative mechanism, multifunctional enzyme, nucleotidyltransferase, uridylation, metal-binding, acyltransferase, catalytic mechanism
• Biological source: HAEMOPHILUS INFLUENZAE
• Cellular location: Cytoplasm (By similarity): P43889
• Total number of polymer chains: 1
• Total formula weight: 50917.24

Authors

Mochalkin, I.,Lightle, S.,Ohren, J.F.,Chirgadze, N.Y. (deposition date: 2007-05-14, release date: 2008-01-15, Last modification date: 2011-07-13)

• Primary citation: Mochalkin, I.,Lightle, S.,Zhu, Y.,Ohren, J.F.,Spessard, C.,Chirgadze, N.Y.,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., 16:2657-, 2007; PubMed: 18029420; DOI: 10.1110/PS.073135107

Experimental method

X-RAY DIFFRACTION (2.3 Å)