6V5E
Crystal structure of CTX-M-14 P167S/D240G beta-lactamase
Summary for 6V5E
Entry DOI | 10.2210/pdb6v5e/pdb |
Descriptor | Beta-lactamase (2 entities in total) |
Functional Keywords | drug resistance, protein evolution, conformational change, enzyme kinetics, enzyme catalysis, protein stability, protein-drug interaction, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 27993.30 |
Authors | Brown, C.A.,Hu, L.,Sankaran, B.,Prasad, B.V.V.,Palzkill, T.G. (deposition date: 2019-12-04, release date: 2020-04-22, Last modification date: 2023-10-11) |
Primary citation | Brown, C.A.,Hu, L.,Sun, Z.,Patel, M.P.,Singh, S.,Porter, J.R.,Sankaran, B.,Prasad, B.V.V.,Bowman, G.R.,Palzkill, T. Antagonism between substitutions in beta-lactamase explains a path not taken in the evolution of bacterial drug resistance. J.Biol.Chem., 295:7376-7390, 2020 Cited by PubMed: 32299911DOI: 10.1074/jbc.RA119.012489 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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