PDBe 1ci8

X-ray diffraction
2Å resolution

ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI: AN ESTERASE WITH (BETA)-LACTAMASE FOLD.

Released:

Function and Biology Details

Reaction catalysed:
A carboxylic ester + H(2)O = an alcohol + a carboxylate. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Esterase EstB Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 41.75 KDa
Source organism: Burkholderia gladioli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KX40 (Residues: 1-392; Coverage: 100%)
Gene name: estB
Sequence domains: Beta-lactamase
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: SIEMENS
Spacegroup: P3221
Unit cell:
a: 82.922Å b: 82.922Å c: 193.46Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.247
Expression system: Escherichia coli