PDBe 3lj6

X-ray diffraction
2.42Å resolution

3D-CRYSTAL STRUCTURE OF HUMANIZED-RAT FATTY ACID AMIDE HYDROLASE (FAAH) CONJUGATED WITH THE DRUG-LIKE UREA INHIBITOR PF-3845 at 2.42A RESOLUTION

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty-acid amide hydrolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 573 amino acids
Theoretical weight: 63.11 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P97612 (Residues: 30-579; Coverage: 95%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 71.59Å b: 105.32Å c: 221.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.2
Expression system: Escherichia coli