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: 2024-05-08) |
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 Cited by PubMed: 18029420DOI: 10.1110/PS.073135107 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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