X-ray diffraction
1.85Å resolution

Crystal Structure of the OXA-48 Carbapenem-Hydrolyzing Class D beta-Lactamase in Complex with the DBO inhibitor ANT3310

Source organism: Klebsiella pneumoniae
Entry authors: Docquier JD, Pozzi C, De Luca F, Benvenuti M, Mangani S

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 30.4 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
  • Canonical: Q6XEC0 (Residues: 1-265; Coverage: 100%)
Gene names: KPE71T_00045, SAMEA3727643_05844, bla OXA-48, blaOXA-48, bla_4
Sequence domains: Penicillin binding protein transpeptidase domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Unit cell:
a: 44.798Å b: 105.106Å c: 125.426Å
α: 90° β: 90° γ: 90°
R R work R free
0.174 0.172 0.218
Expression system: Escherichia coli