› 6v6g

X-ray diffraction
1.5Å resolution

Crystal structure of CTX-M-14 E166A/P167S/D240G beta-lactamase

Released:
DOI: 10.2210/pdb6v6g/pdb
PDB entry 6v6g coloured by chain, front view.
PDB entry 6v6g coloured by chain, side view.
PDB entry 6v6g 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

2 bound ligands:
Ligand PEG 1 x PEG
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P3221
Unit cell:
a: 41.428Å b: 41.428Å c: 231.066Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.183 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

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

1 mention without citation

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