› 4blm

X-ray diffraction
2Å resolution

BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C. REFINEMENT AT 2 ANGSTROMS RESOLUTION AND ANALYSIS OF HYDRATION

Released:
DOI: 10.2210/pdb4blm/pdb
PDB entry 4blm coloured by chain, front view.
PDB entry 4blm coloured by chain, side view.
PDB entry 4blm coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration.
Knox JR, Moews PC
J Mol Biol 220 435-55 (1991)
PMID: 1856867

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 29.54 KDa
Source organism: Bacillus licheniformis
Expression system: Not provided
UniProt:
  • Canonical: P00808 (Residues: 43-307; Coverage: 94%)
Gene names: blaP, penP
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 66.8Å b: 90.7Å c: 43.6Å
α: 90° β: 104.5° γ: 90°
R-values:
R R work R free
0.161 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Catalytic properties of class A beta-lactamases: efficiency and diversity.
Matagne et al. (1998)
3 more

17 mentions without citation

Class A β-lactamases as versatile scaffolds to create hybrid enzymes: applications from basic research to medicine.
Huynen et al. (2013)
16 more