PDBe 2vya

X-ray diffraction
2.75Å resolution

Crystal Structure of fatty acid amide hydrolase conjugated with the drug-like inhibitor PF-750

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: 64.72 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P97612 (Residues: 30-31, 32-579; Coverage: 95%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3221
Unit cell:
a: 103.69Å b: 103.69Å c: 253.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.239
Expression system: Escherichia coli BL21