› 1mbl

X-ray diffraction
2Å resolution

A catalytically-impaired class A beta-lactamase: 2 Angstroms crystal structure and kinetics of the Bacillus licheniformis E166A mutant

Released:
DOI: 10.2210/pdb1mbl/pdb
PDB entry 1mbl coloured by chain, front view.
PDB entry 1mbl coloured by chain, side view.
PDB entry 1mbl coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
A catalytically-impaired class A beta-lactamase: 2 A crystal structure and kinetics of the Bacillus licheniformis E166A mutant.
Knox JR, Moews PC, Escobar WA, Fink AL
Protein Eng 6 11-8 (1993)
PMID: 8433965

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: 256 amino acids
Theoretical weight: 28.43 KDa
Source organism: Bacillus licheniformis
Expression system: Not provided
UniProt:
  • Canonical: P00808 (Residues: 48-303; Coverage: 91%)
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: 67.2Å b: 94.1Å c: 43.8Å
α: 90° β: 104.5° γ: 90°
R-values:
R R work R free
0.182 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
3 more

2 mentions without citation

X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamase.
Risso et al. (2012)
1 more