1mt5

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-161319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty-acid amide hydrolase 1 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 537 amino acids
Theoretical weight: 58.94 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P97612 (Residues: 37-573; Coverage: 93%)
Gene names: Faah, Faah1
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 147.107Å b: 272.019Å c: 147.216Å
α: 90° β: 115.21° γ: 90°
R-values:
R R work R free
0.221 0.218 0.262
Expression system: Escherichia coli BL21