3DJ4

Crystal Structure of GlmU from Mycobacterium tuberculosis in complex with URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE.

Summary for 3DJ4

Entry DOI	10.2210/pdb3dj4/pdb
Related	3DIU
Descriptor	Bifunctional protein glmU, MAGNESIUM ION, COBALT (II) ION, ... (5 entities in total)
Functional Keywords	acetyltransferase, bifunctional, pyrophosphorylase, rossmann-like fold, left-handed-beta-helix, trimer, cell shape, cell wall biogenesis/degradation, cytoplasm, magnesium, metal-binding, multifunctional enzyme, nucleotidyltransferase, peptidoglycan synthesis, transferase, acyltransferase
Biological source	Mycobacterium tuberculosis
Cellular location	Cytoplasm (By similarity): P96382
Total number of polymer chains	1
Total formula weight	52328.32
Authors	Verma, S.K.,Prakash, B. (deposition date: 2008-06-22, release date: 2009-05-19, Last modification date: 2024-03-20)
Primary citation	Parikh, A.,Verma, S.K.,Khan, S.,Prakash, B.,Nandicoori, V.K. PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity. J.Mol.Biol., 386:451-464, 2009 Cited by PubMed: 19121323 DOI: 10.1016/j.jmb.2008.12.031 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.38 Å)

Structure validation