PDBe 1g68

X-ray diffraction
1.95Å resolution

PSE-4 CARBENICILLINASE, WILD TYPE

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase PSE-4 Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 29.56 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P16897 (Residues: 18-288; Coverage: 100%)
Gene names: carB1, pse4
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 95.197Å b: 95.197Å c: 62.793Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 0.212
Expression system: Escherichia coli