X-ray diffraction
2Å resolution

structure of an H300N mutant of potato epoxide hydrolase, StEH1


Function and Biology Details

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 37.13 KDa
Source organism: Solanum tuberosum
Expression system: Escherichia coli
  • Canonical: Q41415 (Residues: 3-321; Coverage: 99%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 56.021Å b: 96.036Å c: 121.551Å
α: 90° β: 90° γ: 90°
R R work R free
0.15 0.147 0.199
Expression system: Escherichia coli