4y0o

X-ray diffraction
2.37Å resolution

Crystal structure of OXA-58, a carbapenem hydrolyzing Class D beta-lactamase from Acinetobacter baumanii.

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174053 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.5 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2TR58 (Residues: 1-280; Coverage: 100%)
Gene names: GSE42_20550, P9867_20895, bla-oxa-58, bla-oxa58, blaOXA-58
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR-H
Spacegroup: P212121
Unit cell:
a: 37.074Å b: 67.038Å c: 93.515Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.193 0.24
Expression system: Escherichia coli BL21