1i2w

X-ray diffraction
1.7Å resolution

BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3 COMPLEXED WITH CEFOXITIN

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-133598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 31.29 KDa
Source organism: Bacillus licheniformis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00808 (Residues: 26-307; Coverage: 100%)
Gene names: blaP, penP
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE D41A
Spacegroup: P21
Unit cell:
a: 47.344Å b: 106.372Å c: 63.873Å
α: 90° β: 94.18° γ: 90°
R-values:
R R work R free
0.216 0.216 0.256
Expression system: Escherichia coli BL21(DE3)