› 2bga

X-ray diffraction
2.7Å resolution

Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH7 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.

Released:
DOI: 10.2210/pdb2bga/pdb
PDB entry 2bga coloured by chain, front view.
PDB entry 2bga coloured by chain, side view.
PDB entry 2bga coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism.
Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM
Biochemistry 44 4841-9 (2005)
PMID: 15779910

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 227 amino acids
Theoretical weight: 24.97 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
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

4 bound ligands:
Ligand AZI 4 x AZI
Ligand GOL 2 x GOL
Ligand ZN 2 x ZN
Ligand SO4 5 x SO4
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P3121
Unit cell:
a: 67.391Å b: 67.391Å c: 178.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 0.248
Expression system: Escherichia coli

Quick links

Citations

4 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
3 more

1 mention without citation

Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?
Oelschlaeger et al. (2010)