2V0I

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

Summary for 2V0I

Entry DOI	10.2210/pdb2v0i/pdb
Related	2V0H 2V0J 2V0K 2V0L
Descriptor	BIFUNCTIONAL PROTEIN GLMU, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, TETRAETHYLENE GLYCOL, ... (6 entities in total)
Functional Keywords	cell wall, cell shape, transferase, peptidoglycan associative mechanism, multifunctional enzyme, nucleotidyltransferase, uridylation, metal-binding, acyltransferase
Biological source	HAEMOPHILUS INFLUENZAE
Cellular location	Cytoplasm (By similarity): P43889
Total number of polymer chains	1
Total formula weight	51024.37
Authors	Mochalkin, I.,Lightle, S.,Ohren, J.F.,Chirgadze, N.Y. (deposition date: 2007-05-14, release date: 2008-01-15, Last modification date: 2023-12-13)
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 Cited by PubMed: 18029420 DOI: 10.1110/PS.073135107 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.89 Å)

Structure validation