5K1F

Crystal structure of a class C beta lactamase/compound2 complex

Summary for 5K1F

• Entry DOI: 10.2210/pdb5k1f/pdb
• Related: 5K1D
• Descriptor: Beta-lactamase, INOSINIC ACID, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: class c beta-lactamase, hydrolase
• Biological source: Enterobacter aerogenes
• Total number of polymer chains: 1
• Total formula weight: 40213.76

Authors

An, Y.J.,Na, J.H.,Cha, S.S. (deposition date: 2016-05-18, release date: 2017-05-17, Last modification date: 2023-11-08)

Primary citation

Na, J.H.,An, Y.J.,Cha, S.S.
GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase.
Antimicrob. Agents Chemother., 61:-, 2017

PubMed Abstract: Nucleotides were effective in inhibiting the class C β-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a value of 16.2 μM. 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.

PubMed: 28242658
DOI: 10.1128/AAC.00098-17

Experimental method

X-RAY DIFFRACTION (1.94 Å)