› 4do3

X-ray diffraction
2.25Å resolution

Structure of FAAH with a non-steroidal anti-inflammatory drug

Released:
DOI: 10.2210/pdb4do3/pdb
PDB entry 4do3 coloured by chain, front view.
PDB entry 4do3 coloured by chain, side view.
PDB entry 4do3 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
A binding site for nonsteroidal anti-inflammatory drugs in fatty acid amide hydrolase.
Bertolacci L, Romeo E, Veronesi M, Magotti P, Albani C, Dionisi M, Lambruschini C, Scarpelli R, Cavalli A, De Vivo M, Piomelli D, Garau G
J Am Chem Soc 135 22-5 (2013)
PMID: 23240907

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: 571 amino acids
Theoretical weight: 62.87 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P97612 (Residues: 32-575; Coverage: 94%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand OHO 2 x OHO
Ligand 0LA 2 x 0LA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 103.47Å b: 104.37Å c: 147.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.199
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Care and feeding of the endocannabinoid system: a systematic review of potential clinical interventions that upregulate the endocannabinoid system.
McPartland et al. (2014)
4 more

9 mentions without citation

A binding site for nonsteroidal anti-inflammatory drugs in fatty acid amide hydrolase.
Bertolacci et al. (2013)
8 more