1y54
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Crystal structure of the native class C beta-lactamase from Enterobacter cloacae 908R complexed with BRL42715
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Structural highlights
FunctionAMPC_ENTCL This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial beta-lactamases. The crystal structure of Enterobacter cloacae 908R class C beta-lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C beta-lactamase. Crystal structure of BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, in complex with Enterobacter cloacae 908R beta-lactamase: evidence for a stereoselective mechanism from docking studies.,Michaux C, Charlier P, Frere JM, Wouters J J Am Chem Soc. 2005 Mar 16;127(10):3262-3. PMID:15755127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 08:00, 15 May 2024.