› 1alq

X-ray diffraction
1.8Å resolution

CIRCULARLY PERMUTED BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1

Released:
DOI: 10.2210/pdb1alq/pdb
PDB entry 1alq coloured by chain, front view.
PDB entry 1alq coloured by chain, side view.
PDB entry 1alq coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Circularly permuted beta-lactamase from Staphylococcus aureus PC1.
Pieper U, Hayakawa K, Li Z, Herzberg O
Biochemistry 36 8767-74 (1997)
PMID: 9220963

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.65 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00807 (Residues: 3-244; Coverage: 86%)
Gene name: blaZ
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand CO3 1 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I222
Unit cell:
a: 53.9Å b: 94.2Å c: 138.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 not available 0.256
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Folding funnels and binding mechanisms.
Ma et al. (1999)
2 more

3 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
2 more