5k1d: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/BLC10_KLEAE BLC10_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).<ref>PMID:15383166</ref> <ref>PMID:16677302</ref> <ref>PMID:28242658</ref> | ||
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== Publication Abstract from PubMed == | |||
Nucleotides 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<ref>PMID:28242658</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 13:30, 1 July 2026
Crystal structure of a class C beta lactamase/compound1 complex
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