2jc7

X-ray diffraction
2.5Å resolution

The crystal structure of the carbapenemase OXA-24 reveals new insights into the mechanism of carbapenem-hydrolysis

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-186001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.54 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8RLA6 (Residues: 32-275; Coverage: 96%)
Gene names: APD33_00525, MKP18_004229, MKP18_004230, MKP18_004396, MKP18_004397, 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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P41212
Unit cell:
a: 102.2Å b: 102.2Å c: 86.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.234
Expression system: Escherichia coli BL21(DE3)