› 3qkv

X-ray diffraction
3.1Å resolution

Crystal structure of fatty acid amide hydrolase with small molecule compound

Released:
DOI: 10.2210/pdb3qkv/pdb
PDB entry 3qkv coloured by chain, front view.
PDB entry 3qkv coloured by chain, side view.
PDB entry 3qkv coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH).
Min X, Thibault ST, Porter AC, Gustin DJ, Carlson TJ, Xu H, Lindstrom M, Xu G, Uyeda C, Ma Z, Li Y, Kayser F, Walker NP, Wang Z
Proc Natl Acad Sci U S A 108 7379-84 (2011)
PMID: 21502526

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: 587 amino acids
Theoretical weight: 64.59 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P97612 (Residues: 32-579; Coverage: 95%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

1 bound ligand:
Ligand QKV 2 x QKV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 90.82Å b: 104.08Å c: 147.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.268 0.266 0.289
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

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

2 mentions without citation

Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH).
Min et al. (2011)
1 more