5k1d
Crystal structure of a class C beta lactamase/compound1 complex
Structural highlights
FunctionBLC10_KLEAE Class C beta-lactamase which confers resistance to penicillins and cephalosporins (PubMed:15383166). Has benzylpenicillin-, ceftazidime-, nitrocefin- and imipenem-hydrolyzing activity (PubMed:16677302, PubMed:28242658).[1] [2] [3] Publication Abstract from PubMedNucleotides were effective in inhibiting the class C beta-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a Ki value of 16.2 muM. The crystal structure of CMY-10 complexed with GMP or IMP revealed that nucleotides fit into the R2 subsite of the active site with a unique vertical binding mode where the phosphate group at one terminus is deeply bound in the subsite and the base at the other terminus faces the solvent. GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase.,Na JH, An YJ, Cha SS Antimicrob Agents Chemother. 2017 Apr 24;61(5). pii: e00098-17. doi:, 10.1128/AAC.00098-17. Print 2017 May. PMID:28242658[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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