› 6i5e

X-ray diffraction
2.6Å resolution

X-ray structure of apo human soluble Epoxide Hydrolase C-terminal Domain (hsEH CTD)

Released:
DOI: 10.2210/pdb6i5e/pdb
PDB entry 6i5e coloured by chain, front view.
PDB entry 6i5e coloured by chain, side view.
PDB entry 6i5e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
15-deoxy-Δ12,14-Prostaglandin J2 inhibits human soluble epoxide hydrolase by a dual orthosteric and allosteric mechanism.
Abis G, Charles RL, Kopec J, Yue WW, Atkinson RA, Bui TTT, Lynham S, Popova S, Sun YB, Fraternali F, Eaton P, Conte MR
Commun Biol 2 188 (2019)
PMID: 31123712

Function and Biology Details

Reactions catalysed: 
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
An epoxide + H(2)O = a glycol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional epoxide hydrolase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 39.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P34913 (Residues: 230-555; Coverage: 59%)
Gene name: EPHX2
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: DIAMOND BEAMLINE I04
Unit cell:
a: 88.224Å b: 80.139Å c: 104.696Å
α: 90° β: 95.39° γ: 90°
R-values:
R R work R free
0.248 0.246 0.277
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Nrf2-A Molecular Target for Sepsis Patients in Critical Care.
Gunne et al. (2020)
2 more

1 mention without citation

A thiol redox sensor in soluble epoxide hydrolase enables oxidative activation by intra-protein disulfide bond formation.
Charles et al. (2021)