3NWY

Structure and allosteric regulation of the uridine monophosphate kinase from Mycobacterium tuberculosis

Summary for 3NWY

Entry DOI	10.2210/pdb3nwy/pdb
Descriptor	Uridylate kinase, GUANOSINE-5'-TRIPHOSPHATE, URIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywords	allosterically activated form, aak fold, ump kinase, transferase
Biological source	Mycobacterium tuberculosis
Cellular location	Cytoplasm (By similarity): P65929
Total number of polymer chains	6
Total formula weight	181298.60
Authors	Labesse, G.,Munier-Lehmann, H. (deposition date: 2010-07-12, release date: 2010-08-25, Last modification date: 2024-04-03)
Primary citation	Labesse, G.,Benkali, K.,Salard-Arnaud, I.,Gilles, A.M.,Munier-Lehmann, H. Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation. Nucleic Acids Res., 39:3458-3472, 2011 Cited by PubMed: 21149268 DOI: 10.1093/nar/gkq1250 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.54 Å)

Structure validation