2c7b

X-ray diffraction
2.3Å resolution

The Crystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-177140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 311 amino acids
Theoretical weight: 34.06 KDa
Source organism: uncultured archaeon
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5G935 (Residues: 1-311; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P41212
Unit cell:
a: 73.71Å b: 73.71Å c: 234.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.261
Expression system: Escherichia coli BL21(DE3)