4HCQ
Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate
Summary for 4HCQ
Entry DOI | 10.2210/pdb4hcq/pdb |
Descriptor | Bifunctional protein GlmU, 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose, COBALT (II) ION, ... (5 entities in total) |
Functional Keywords | acetyltransferase, bifunctional, pyrophosphorylase, rossmann-like fold, left-handed-beta-helix, cell shape, cell wall biogenesis/degradation, magnesium, metal-binding, multifunctional enzyme, nucleotidyltransferase, peptidoglycan synthesis, transferase, acyltransferase |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 53176.52 |
Authors | Jagtap, P.K.A.,Verma, S.K.,Vithani, N. (deposition date: 2012-10-01, release date: 2013-03-13, Last modification date: 2023-11-08) |
Primary citation | Jagtap, P.K.A.,Verma, S.K.,Vithani, N.,Bais, V.S.,Prakash, B. Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases J.Mol.Biol., 425:1745-1759, 2013 Cited by PubMed: 23485416DOI: 10.1016/j.jmb.2013.02.019 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report