8AKI
Acyl-enzyme complex of ampicillin bound to deacylation mutant KPC-2 (E166Q)
Summary for 8AKI
Entry DOI | 10.2210/pdb8aki/pdb |
Descriptor | Carbapenem-hydrolyzing beta-lactamase KPC, (2R,4S)-2-[(1R)-1-{[(2R)-2-amino-2-phenylacetyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid, SULFATE ION, ... (5 entities in total) |
Functional Keywords | acyl-enzyme complex, antibiotic resistance, beta-lactamase, antibiotic, ligand, antimicrobial protein |
Biological source | Klebsiella pneumoniae |
Total number of polymer chains | 1 |
Total formula weight | 31633.41 |
Authors | Tooke, C.L.,Hinchliffe, P.,Spencer, J. (deposition date: 2022-07-29, release date: 2023-03-08, Last modification date: 2024-02-07) |
Primary citation | Tooke, C.L.,Hinchliffe, P.,Beer, M.,Zinovjev, K.,Colenso, C.K.,Schofield, C.J.,Mulholland, A.J.,Spencer, J. Tautomer-Specific Deacylation and Omega-Loop Flexibility Explain the Carbapenem-Hydrolyzing Broad-Spectrum Activity of the KPC-2 beta-Lactamase. J.Am.Chem.Soc., 145:7166-7180, 2023 Cited by PubMed: 36972204DOI: 10.1021/jacs.2c12123 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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