› 1pio

X-ray diffraction
2.8Å resolution

AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS

Released:
DOI: 10.2210/pdb1pio/pdb
PDB entry 1pio coloured by chain, front view.
PDB entry 1pio coloured by chain, side view.
PDB entry 1pio coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins.
Zawadzke LE, Smith TJ, Herzberg O
Protein Eng 8 1275-85 (1995)
PMID: 8869640

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 28.88 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00807 (Residues: 25-281; Coverage: 100%)
Gene name: blaZ
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 54Å b: 67.6Å c: 141.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.189
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Catalytic properties of class A beta-lactamases: efficiency and diversity.
Matagne et al. (1998)
8 other articles