1KVM

X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin

Summary for 1KVM

• Entry DOI: 10.2210/pdb1kvm/pdb
• Related: 1KE4 1KVL 2BLS
• Descriptor: beta-lactamase, PHOSPHATE ION, 5-METHYLENE-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID, ... (4 entities in total)
• Functional Keywords: amide hydrolase, beta-lactamase, cephalothin, acyl-enzyme complex, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00811
• Total number of polymer chains: 2
• Total formula weight: 79609.22

Authors

Beadle, B.M.,Trehan, I.,Focia, P.J.,Shoichet, B.K. (deposition date: 2002-01-27, release date: 2002-03-13, Last modification date: 2023-08-16)

• Primary citation: Beadle, B.M.,Trehan, I.,Focia, P.J.,Shoichet, B.K.; Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.; Structure, 10:413-424, 2002; PubMed: 12005439; DOI: 10.1016/S0969-2126(02)00725-6

Experimental method

X-RAY DIFFRACTION (2.06 Å)