› 3i0v

X-ray diffraction
1.6Å resolution

Bacillus cereus metallo-beta-lactamase: apo form

Released:
DOI: 10.2210/pdb3i0v/pdb
PDB entry 3i0v coloured by chain, front view.
PDB entry 3i0v coloured by chain, side view.
PDB entry 3i0v coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .
González JM, Buschiazzo A, Vila AJ
Biochemistry 49 7930-8 (2010)
PMID: 20677753

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 25.04 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli BL21(DE3)
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

No bound ligands
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 53.039Å b: 61.627Å c: 69.528Å
α: 90° β: 92.98° γ: 90°
R-values:
R R work R free
0.163 0.161 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

A variety of roles for versatile zinc in metallo-β-lactamases.
Karsisiotis et al. (2014)
2 more

3 mentions without citation

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
2 more