› 6b22

X-ray diffraction
1.93Å resolution

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-186001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-binding protein transpeptidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.54 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RLA6 (Residues: 32-275; Coverage: 96%)
Gene names: APD17_12635, MKP18_004229, MKP18_004396, bla-OXA-40, blaOXA-24, blaOXA-33, blaOXA-40, oxa-24, oxa40
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand C8Y 1 x C8Y
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P41212
Unit cell:
a: 102.539Å b: 102.539Å c: 84.312Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.198
Expression system: Escherichia coli

Quick links

Citations

31 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
30 more

1 mention without citation

Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234.
Papp-Wallace et al. (2018)