2V0L

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

Summary for 2V0L

Entry DOI	10.2210/pdb2v0l/pdb
Related	2V0H 2V0I 2V0J 2V0K
Descriptor	BIFUNCTIONAL PROTEIN GLMU, URIDINE, TETRAETHYLENE GLYCOL, ... (6 entities in total)
Functional Keywords	glmu, cell wall, magnesium, cell shape, transferase, peptidoglycan synthesis, multifunctional enzyme, nucleotidyltransferase, uridylation, metal-binding, acyltransferase, catalytic mechanism, associative mechanism
Biological source	HAEMOPHILUS INFLUENZAE
Cellular location	Cytoplasm (By similarity): P43889
Total number of polymer chains	1
Total formula weight	50757.28
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 (2.2 Å)

Structure validation