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 Cited by PubMed: 12005439DOI: 10.1016/S0969-2126(02)00725-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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