PDBe 4hbp

X-ray diffraction
2.91Å resolution

Crystal Structure of FAAH in complex with inhibitor

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: 550 amino acids
Theoretical weight: 60.53 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P97612 (Residues: 30-579; Coverage: 95%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P3221
Unit cell:
a: 103.92Å b: 103.92Å c: 251.965Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.223 0.273
Expression system: Escherichia coli