2uyx

X-ray diffraction
1.95Å resolution

metallo-beta-lactamase (1BC2) single point mutant D120S

Released:
Source organism: Bacillus cereus
Primary publication:
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity.
J Biol Chem 282 18276-18285 (2007)
PMID: 17426028

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:
monomeric (preferred)
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: 228 amino acids
Theoretical weight: 25.04 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04190 (Residues: 30-257; Coverage: 100%)
Gene name: blm
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: C2
Unit cell:
a: 53.389Å b: 61.97Å c: 69.573Å
α: 90° β: 93.28° γ: 90°
R-values:
R R work R free
0.15 0.146 0.221
Expression system: Escherichia coli BL21(DE3)