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X-ray diffraction
2.07Å resolution

CRYSTAL STRUCTURE OF THE BETA-LACTAMASE OXA-163

Released:
DOI: 10.2210/pdb5odz/pdb
PDB entry 5odz coloured by chain, front view.
PDB entry 5odz coloured by chain, side view.
PDB entry 5odz coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis.
Lund BA, Thomassen AM, Carlsen TJO, Leiros HKS
Acta Crystallogr F Struct Biol Commun 73 579-587 (2017)
PMID: 28994407

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-123623 (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:
Ligand CL 4 x CL
Ligand MG 3 x MG
Ligand PGE 1 x PGE
1 modified residue:
Ligand KCX 2 x KCX

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)

Quick links

Citations

1 review citation

The Global Ascendency of OXA-48-Type Carbapenemases.
Pitout et al. (2019)
7 other articles

1 mention without citation

Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis.
Lund et al. (2017)