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2V0J

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

Summary for 2V0J
Entry DOI10.2210/pdb2v0j/pdb
Related2V0H 2V0I 2V0K 2V0L
DescriptorBIFUNCTIONAL PROTEIN GLMU, 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE, MAGNESIUM ION, ... (7 entities in total)
Functional Keywordsglmu, cell wall, magnesium, cell shape, transferase, peptidoglycan synthesis, associative mechanism, multifunctional enzyme, nucleotidyltransferase, uridylation, metal-binding, acyltransferase, catalytic mechanism
Biological sourceHAEMOPHILUS INFLUENZAE
Cellular locationCytoplasm (By similarity): P43889
Total number of polymer chains1
Total formula weight50791.82
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 citationMochalkin, 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 Å)
Structure validation

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