PDBe 1nu3

X-ray diffraction
1.75Å resolution

Limonene-1,2-epoxide hydrolase in complex with valpromide

Released:

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
Macromolecule:
Limonene-1,2-epoxide hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 16.69 KDa
Source organism: Rhodococcus erythropolis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZAG3 (Residues: 1-149; Coverage: 100%)
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:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 45.596Å b: 47.656Å c: 129.244Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.195
Expression system: Escherichia coli