5A92
15K X-ray structure with Cefotaxime: Exploring the Mechanism of beta- Lactam Ring Protonation in the Class A beta-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography
Summary for 5A92
Entry DOI | 10.2210/pdb5a92/pdb |
Related | 5A90 5A91 5A93 |
Descriptor | BETA-LACTAMASE CTX-M-97, SULFATE ION, CEFOTAXIME, C3' cleaved, open, bound form, ... (4 entities in total) |
Functional Keywords | hydrolase, beta lactamase |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 1 |
Total formula weight | 28995.50 |
Authors | Vandavasi, V.G.,Weiss, K.L.,Cooper, J.B.,Erskine, P.T.,Tomanicek, S.J.,Ostermann, A.,Schrader, T.E.,Ginell, S.L.,Coates, L. (deposition date: 2015-07-17, release date: 2015-12-16, Last modification date: 2018-10-03) |
Primary citation | Vandavasi, V.G.,Weiss, K.L.,Cooper, J.B.,Erskine, P.T.,Tomanicek, S.J.,Ostermann, A.,Schrader, T.E.,Ginell, S.L.,Coates, L. Exploring the Mechanism of Beta-Lactam Ring Protonation in the Class a Beta-Lactamase Acylation Mechanism Using Neutron and X-Ray Crystallography. J.Med.Chem., 59:474-, 2016 Cited by PubMed: 26630115DOI: 10.1021/ACS.JMEDCHEM.5B01215 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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