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: 26630115 DOI: 10.1021/ACS.JMEDCHEM.5B01215 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.05 Å)

Structure validation