› 3k84

X-ray diffraction
2.25Å resolution

Crystal Structure Analysis of a Oleyl/Oxadiazole/pyridine Inhibitor Bound to a Humanized Variant of Fatty Acid Amide Hydrolase

Released:
DOI: 10.2210/pdb3k84/pdb
PDB entry 3k84 coloured by chain, front view.
PDB entry 3k84 coloured by chain, side view.
PDB entry 3k84 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
X-ray crystallographic analysis of alpha-ketoheterocycle inhibitors bound to a humanized variant of fatty acid amide hydrolase.
Mileni M, Garfunkle J, Ezzili C, Kimball FS, Cravatt BF, Stevens RC, Boger DL
J Med Chem 53 230-40 (2010)
PMID: 19924997

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
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 K84 2 x K84
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: 104.05Å b: 104.05Å c: 255.32Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.166 0.211
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH).
Otrubova et al. (2011)
3 more

6 mentions without citation

X-ray crystallographic analysis of alpha-ketoheterocycle inhibitors bound to a humanized variant of fatty acid amide hydrolase.
Mileni et al. (2010)
5 more