› 3aik

X-ray diffraction
1.95Å resolution

Crystal structure of a HSL-like carboxylesterase from Sulfolobus tokodaii

Released:
DOI: 10.2210/pdb3aik/pdb
PDB entry 3aik coloured by chain, front view.
PDB entry 3aik coloured by chain, side view.
PDB entry 3aik 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 MPD 4 x MPD
Ligand MRD 6 x MRD
Ligand PO4 5 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P21
Unit cell:
a: 76.327Å b: 114.752Å c: 102.206Å
α: 90° β: 108.84° γ: 90°
R-values:
R R work R free
0.161 0.159 0.194
Expression system: Escherichia coli

Quick links

Citations

18 citation in other articles

Biochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira sp.
De Santi et al. (2016)
17 more

11 mentions without citation

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)
10 more