X-ray diffraction
1.5Å resolution

Structure of thermostable eightfold mutant of limonene epoxide hydrolase from Rhodococcus erythropolis


Function and Biology Details

Reaction catalysed:
1,2-epoxymenth-8-ene + H(2)O = menth-8-ene-1,2-diol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Limonene-1,2-epoxide hydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 174 amino acids
Theoretical weight: 19.48 KDa
Source organism: Rhodococcus erythropolis
Expression system: Escherichia coli
  • Canonical: Q9ZAG3 (Residues: 3-149; Coverage: 99%)
Gene name: limA
Sequence domains: Limonene-1,2-epoxide hydrolase catalytic domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 88.049Å b: 88.049Å c: 110.241Å
α: 90° β: 90° γ: 120°
R R work R free
0.143 0.141 0.165
Expression system: Escherichia coli