› 3ail

X-ray diffraction
1.91Å resolution

Crystal structure of a HSL-like carboxylesterase from Sulfolobus tokodaii complexed with paraoxon

Released:
DOI: 10.2210/pdb3ail/pdb
PDB entry 3ail coloured by chain, front view.
PDB entry 3ail coloured by chain, side view.
PDB entry 3ail coloured by chain, top view.
Source organism: Sulfurisphaera tokodaii
Primary publication:
Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii.
Angkawidjaja C, Koga Y, Takano K, Kanaya S
FEBS J 279 3071-84 (2012)
PMID: 22748144

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 323 amino acids
Theoretical weight: 36.01 KDa
Source organism: Sulfurisphaera tokodaii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q976W8 (Residues: 1-303; Coverage: 100%)
Gene names: ST0071, STK_00710
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand DEP 4 x DEP
Ligand MRD 4 x MRD
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 76.323Å b: 114.367Å c: 101.892Å
α: 90° β: 108.44° γ: 90°
R-values:
R R work R free
0.164 0.162 0.191
Expression system: Escherichia coli

Quick links

Citations

26 citation in other articles

Structural basis for dimerization and catalysis of a novel esterase from the GTSAG motif subfamily of the bacterial hormone-sensitive lipase family.
Li et al. (2014)
25 more

1 mention without citation

Identification of interactions in the E1E2 heterodimer of hepatitis C virus important for cell entry.
Maurin et al. (2011)