3FOQ
Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.
Summary for 3FOQ
| Entry DOI | 10.2210/pdb3foq/pdb |
| Related | 3DK5 |
| Descriptor | Bifunctional protein glmU, SULFATE ION (2 entities in total) |
| Functional Keywords | acetyltransferase, bifunctional, pyrophosphorylase, rossmann-like fold, left-handed-beta-helix, trimer, acyltransferase, cell shape, cell wall biogenesis/degradation, cytoplasm, magnesium, metal-binding, multifunctional enzyme, nucleotidyltransferase, peptidoglycan synthesis, transferase |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (By similarity): P96382 |
| Total number of polymer chains | 1 |
| Total formula weight | 53111.23 |
| Authors | Verma, S.K.,Prakash, B. (deposition date: 2008-12-31, release date: 2009-06-09, Last modification date: 2024-03-20) |
| Primary citation | Verma, S.K.,Jaiswal, M.,Kumar, N.,Parikh, A.,Nandicoori, V.K.,Prakash, B. Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group. Acta Crystallogr.,Sect.F, 65:435-439, 2009 Cited by PubMed: 19407371DOI: 10.1107/S1744309109010252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.41 Å) |
Structure validation
Download full validation report
