4E1K
GlmU in complex with a Quinazoline Compound
Summary for 4E1K
Entry DOI | 10.2210/pdb4e1k/pdb |
Descriptor | Bifunctional protein GlmU, SULFATE ION, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | peptidoglycan synthesis, cell shape, metal-binding, cell wall biogenesis/degradation, multifunctional enzyme, acyltransferase, uridyltransferase, nucleotidyl transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
Biological source | Haemophilus influenzae |
Cellular location | Cytoplasm (By similarity): P43889 |
Total number of polymer chains | 1 |
Total formula weight | 50214.88 |
Authors | Larsen, N.A.,Doig, P. (deposition date: 2012-03-06, release date: 2013-05-29, Last modification date: 2024-02-28) |
Primary citation | Larsen, N.A.,Nash, T.J.,Morningstar, M.,Shapiro, A.B.,Joubran, C.,Blackett, C.J.,Patten, A.D.,Boriack-Sjodin, P.A.,Doig, P. An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode. Biochem.J., 446:405-413, 2012 Cited by PubMed: 22721802DOI: 10.1042/BJ20120596 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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