› 3oj8

X-ray diffraction
1.9Å resolution

Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints in the Acyl Side Chain

Released:
DOI: 10.2210/pdb3oj8/pdb
PDB entry 3oj8 coloured by chain, front view.
PDB entry 3oj8 coloured by chain, side view.
PDB entry 3oj8 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Reversible competitive ��-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational constraints in the acyl side chain: orally active, long-acting analgesics.
Ezzili C, Mileni M, McGlinchey N, Long JZ, Kinsey SG, Hochstatter DG, Stevens RC, Lichtman AH, Cravatt BF, Bilsky EJ, Boger DL
J. Med. Chem. 54 2805-22 (2011)
PMID: 21428410

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161319 (preferred)
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 BL21
UniProt:
  • Canonical: 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:
Ligand OJ8 2 x OJ8
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P3221
Unit cell:
a: 103.299Å b: 103.299Å c: 253.355Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.154 0.185
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Chemical probes of endocannabinoid metabolism.
Blankman et al. (2013)
3 more

1 mention without citation

Reversible competitive α-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational constraints in the acyl side chain: orally active, long-acting analgesics.
Ezzili et al. (2011)