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: 19121323DOI: 10.1016/j.jmb.2008.12.031 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
Download full validation report