3DK5
Crystal Structure of Apo-GlmU from Mycobacterium tuberculosis
Summary for 3DK5
| Entry DOI | 10.2210/pdb3dk5/pdb |
| Related | 3DIU 3DJ4 |
| Descriptor | Bifunctional protein glmU, MAGNESIUM ION (3 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 |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (By similarity): A5U161 |
| Total number of polymer chains | 1 |
| Total formula weight | 51686.34 |
| Authors | Verma, S.K.,Prakash, B. (deposition date: 2008-06-24, 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 (2.23 Å) |
Structure validation
Download full validation report
