8PEC
OXA-48_Q5-CAZ. Epistasis Arises from Shifting the Rate-Limiting Step during Enzyme Evolution
Summary for 8PEC
Entry DOI | 10.2210/pdb8pec/pdb |
Descriptor | Beta-lactamase, 1-({(2R)-2-[(1R)-1-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}-2-oxoethyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-5-yl}methyl)pyridinium, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | protein evolution. antibiotic resistance. oxa-48. hydrolase. serine-beta-lactamase., hydrolase |
Biological source | Klebsiella pneumoniae |
Total number of polymer chains | 4 |
Total formula weight | 113730.56 |
Authors | Leiros, H.-K.S.,Frohlich, C. (deposition date: 2023-06-13, release date: 2024-02-14, Last modification date: 2024-06-12) |
Primary citation | Frohlich, C.,Bunzel, H.A.,Buda, K.,Mulholland, A.J.,van der Kamp, M.W.,Johnsen, P.J.,Leiros, H.S.,Tokuriki, N. Epistasis arises from shifting the rate-limiting step during enzyme evolution of a beta-lactamase. Nat Catal, 7:499-509, 2024 Cited by PubMed: 38828429DOI: 10.1038/s41929-024-01117-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.66 Å) |
Structure validation
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