› 5faq

X-ray diffraction
1.96Å 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.93 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6XEC0 (Residues: 25-265; Coverage: 99%)
Gene names: AI2879V1_5232, GJJ21_26815, KPE71T_00045, SAMEA3727706_05517, bla OXA-48, blaOXA-48, bla_4
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

4 bound ligands:
Ligand CD 3 x CD
Ligand CL 1 x CL
Ligand 5VW 2 x 5VW
Ligand CO 6 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 72.76Å b: 75.47Å c: 106.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.21
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

1 mention without citation

Antimicrobial Resistance Conferred by OXA-48 β-Lactamases: Towards a Detailed Mechanistic Understanding.
Hirvonen et al. (2021)