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-Structure paper
Title | Mutagenesis and structural analysis reveal the CTX-M beta-lactamase active site is optimized for cephalosporin catalysis and drug resistance. |
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Journal, issue, pages | J. Biol. Chem., Vol. 299, Page 104630-104630, Year 2023 |
Publish date | Jul 12, 2022 (structure data deposition date) |
![]() | Lu, S. / Montoya, M. / Hu, L. / Neetu, N. / Sankaran, B. / Prasad, B.V.V. / Palzkill, T. |
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Methods | X-ray diffraction |
Resolution | 1.36 - 1.67 Å |
Structure data | ![]() PDB-8dod: ![]() PDB-8doe: ![]() PDB-8don: ![]() PDB-8dp4: ![]() PDB-8dpq: ![]() PDB-8ela: ![]() PDB-8elb: |
Chemicals | ![]() ChemComp-K: ![]() ChemComp-HOH: ![]() ChemComp-PO4: ![]() ChemComp-EDO: ![]() ChemComp-MES: ![]() ChemComp-SO4: ![]() ChemComp-ZN: ![]() ChemComp-CL: ![]() ChemComp-PEG: |
Source |
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![]() | HYDROLASE / Beta-lactamase / CTX-M-14 / mutation / B-lactam / antibiotic resistance / b-lactam antibiotic resistance / Beta-lactam / beta-lactamase antibiotic beta-lactam / beta-lactamase hydrolase antibiotic beta-lactam |