5odz

X-ray diffraction
2.07Å resolution

CRYSTAL STRUCTURE OF THE BETA-LACTAMASE OXA-163

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: B, D
Molecule details ›
Chains: B, D
Length: 252 amino acids
Theoretical weight: 29.44 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F6KZJ2 (Residues: 23-261; Coverage: 100%)
Gene name: blaOXA-163
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6522
Unit cell:
a: 121.92Å b: 121.92Å c: 160.426Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.145 0.187
Expression system: Escherichia coli BL21(DE3)