› 6v7t

X-ray diffraction
1.34Å resolution

Crystal structure of CTX-M-14 E166A/D240G beta-lactamase in complex with ceftazidime

Released:
DOI: 10.2210/pdb6v7t/pdb
PDB entry 6v7t coloured by chain, front view.
PDB entry 6v7t coloured by chain, side view.
PDB entry 6v7t coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance.
Brown CA, Hu L, Sun Z, Patel MP, Singh S, Porter JR, Sankaran B, Prasad BVV, Bowman GR, Palzkill T
J Biol Chem 295 7376-7390 (2020)
PMID: 32299911

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

1 bound ligand:
Ligand CAZ 2 x CAZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 45.11Å b: 107.33Å c: 47.75Å
α: 90° β: 99.86° γ: 90°
R-values:
R R work R free
0.144 0.143 0.162
Expression system: Escherichia coli BL21(DE3)

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Citations

8 citation in other articles

Natural variants modify Klebsiella pneumoniae carbapenemase (KPC) acyl-enzyme conformational dynamics to extend antibiotic resistance.
Tooke et al. (2021)
7 more

2 mentions without citation

Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance.
Brown et al. (2020)
1 more