› 1bc2

X-ray diffraction
1.9Å resolution

ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS

Released:
DOI: 10.2210/pdb1bc2/pdb
PDB entry 1bc2 coloured by chain, front view.
PDB entry 1bc2 coloured by chain, side view.
PDB entry 1bc2 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ
Biochemistry 37 12404-11 (1998)
PMID: 9730812

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 227 amino acids
Theoretical weight: 25 KDa
Source organism: Bacillus cereus
UniProt:
  • Canonical: P04190 (Residues: 31-257; Coverage: 100%)
Gene name: blm
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P3121
Unit cell:
a: 67.63Å b: 67.63Å c: 178.38Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.279

Quick links

Citations

13 review citations

Carbapenemases: the versatile beta-lactamases.
Queenan et al. (2007)
12 more

22 mentions without citation

Overcoming differences: The catalytic mechanism of metallo-β-lactamases.
Meini et al. (2015)
21 more