PDBe 3qj8

X-ray diffraction
2.9Å resolution

Crystal structure of fatty acid amide hydrolase

Released:

Function and Biology Details

Reaction catalysed:
Anandamide + H(2)O = arachidonic acid + ethanolamine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty-acid amide hydrolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 587 amino acids
Theoretical weight: 64.59 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P97612 (Residues: 32-579; Coverage: 95%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 91.54Å b: 104.62Å c: 148.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.217 0.262
Expression system: Escherichia coli BL21