9TLD

Cefdinir bound Class A CTX-M-14 mutant E166A at Cryo SSX

This is a non-PDB format compatible entry.

Summary for 9TLD

• Entry DOI: 10.2210/pdb9tld/pdb
• Descriptor: Beta-lactamase, Cefdinir, bound form (3 entities in total)
• Functional Keywords: cephalosporin, ctx-m-14, antibiotic
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 27997.55

Authors

Gore, G.,Schulz, E.C. (deposition date: 2025-12-10, release date: 2026-10-21)

Primary citation

Gore, G.,Prester, A.,Bartels, K.,von Stetten, D.,Schulz, E.C.
Cefdinir binding to a class A beta-lactamase revealed by serial cryo-crystallography.
Acta Crystallogr D Struct Biol, 82:672-682, 2026

PubMed Abstract: One of the most common resistance mechanisms against antibiotics employed by Gram-negative bacteria involves the production of β-lactamases, resulting in rapid hydrolysis of the antibiotic. Extensive use of the early-generation cephalosporins led to the rise of extended-spectrum β-lactamases such as CTX-Ms. Cefdinir is an extended-spectrum third-generation cephalosporin administered since the late 1990s; despite this, there is no reported 3D structure of the antibiotic bound to any β-lactamase or penicillin-binding protein in the PDB. Here, we report the X-ray crystallographic structure of cefdinir-bound CTX-M-14 E166A mutant obtained via serial cryo-crystallography.

PubMed: 42158994
DOI: 10.1107/S2059798326003992

Experimental method

X-RAY DIFFRACTION (1.6 Å)