5G18

Direct Observation of Active-site Protonation States in a Class A beta lactamase with a monobactam substrate

Summary for 5G18

Entry DOI	10.2210/pdb5g18/pdb
Descriptor	BETA-LACTAMASE CTX-M-97, 2-({[(1Z)-1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-{[(2S,3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino}ethylidene]amino}oxy)-2-methylpropanoic acid, SULFATE ION, ... (4 entities in total)
Functional Keywords	hydrolase, beta lactamase, toho, neutron
Biological source	ESCHERICHIA COLI
Total number of polymer chains	1
Total formula weight	29035.52
Authors	Vandavasi, V.G.,Weiss, K.L.,Parks, J.M.,Cooper, J.B.,Ginell, S.L.,Coates, L. (deposition date: 2016-03-23, release date: 2016-11-09, Last modification date: 2019-10-23)
Primary citation	Vandavasi, V.G.,Langan, P.S.,Weiss, K.L.,Parks, J.M.,Cooper, J.B.,Ginell, S.L.,Coates, L. Active-Site Protonation States in an Acyl-Enzyme Intermediate of a Class A beta-Lactamase with a Monobactam Substrate. Antimicrob. Agents Chemother., 61:-, 2017 Cited by PubMed: 27795378 DOI: 10.1128/AAC.01636-16 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.1 Å)

Structure validation