X-ray diffraction
1.16Å resolution

Structural studies of a thermophilic esterase from Thermogutta terrifontis (malate bound)


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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 31.17 KDa
Source organism: Thermogutta terrifontis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A0M3KKY6 (Residues: 1-282; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 43.33Å b: 43.33Å c: 227.06Å
α: 90° β: 90° γ: 120°
R R work R free
0.109 0.107 0.142
Expression system: Escherichia coli BL21(DE3)