› 1ci8

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb1ci8/pdb
PDB entry 1ci8 coloured by chain, front view.
PDB entry 1ci8 coloured by chain, side view.
PDB entry 1ci8 coloured by chain, top view.
Source organism: Burkholderia gladioli
Primary publication:
EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity.
Wagner UG, Petersen EI, Schwab H, Kratky C
Protein Sci 11 467-78 (2002)
PMID: 11847270

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192170 (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:
Ligand IPA 4 x IPA
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

Quick links

Citations

4 review citations

Enzymatic synthesis of optically active tertiary alcohols: expanding the biocatalysis toolbox.
Kourist et al. (2008)
3 more

7 mentions without citation

EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity.
Wagner et al. (2002)
6 more