› 2vya

X-ray diffraction
2.75Å resolution

Crystal Structure of fatty acid amide hydrolase conjugated with the drug-like inhibitor PF-750

Released:
DOI: 10.2210/pdb2vya/pdb
PDB entry 2vya coloured by chain, front view.
PDB entry 2vya coloured by chain, side view.
PDB entry 2vya coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure-guided inhibitor design for human FAAH by interspecies active site conversion.
Mileni M, Johnson DS, Wang Z, Everdeen DS, Liimatta M, Pabst B, Bhattacharya K, Nugent RA, Kamtekar S, Cravatt BF, Ahn K, Stevens RC
Proc Natl Acad Sci U S A 105 12820-4 (2008)
PMID: 18753625

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: 64.72 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P97612 (Residues: 30-31, 32-579; Coverage: 95%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

3 bound ligands:
Ligand UNX 4 x UNX
Ligand PF7 2 x PF7
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3221
Unit cell:
a: 103.69Å b: 103.69Å c: 253.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.239
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Biology-inspired microphysiological system approaches to solve the prediction dilemma of substance testing.
Marx et al. (2016)
7 more

14 mentions without citation

Structure-guided inhibitor design for human FAAH by interspecies active site conversion.
Mileni et al. (2008)
13 more