› 1qo7

X-ray diffraction
1.8Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epoxide hydrolase N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 44.12 KDa
Source organism: Aspergillus niger
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UR30 (Residues: 3-396; Coverage: 99%)
Gene name: hyl1
Sequence domains: Epoxide hydrolase N terminus
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 ID14-4
Spacegroup: P21
Unit cell:
a: 62.69Å b: 89.32Å c: 75.77Å
α: 90° β: 105.37° γ: 90°
R-values:
R R work R free
0.224 0.224 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

Lipolysis - a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores.
Lass et al. (2011)
25 more

5 mentions without citation

The N-terminal region of comparative gene identification-58 (CGI-58) is important for lipid droplet binding and activation of adipose triglyceride lipase.
Gruber et al. (2010)
4 more