Cloned (Comment) | Organism |
---|---|
expression of His-tagged FAAH in Escherichia coli strain | Rattus norvegicus |
expression of His-tagged FAAH in Escherichia coli strain | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
purified recombinant His-tagged apo FAAH, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement | Rattus norvegicus |
purified recombinant His-tagged apo FAAH, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one | the compound belongs to the ketobenzimidazoles, though containing a carbonyl moiety, that do not covalently modify Ser241. These inhibitors achieve potent inhibition of FAAH activity primarily from shape complementarity to the active site and through numerous hydrophobic interactions exhibiting excellent selectivity and good pharmacokinetic properties, nonmechanism-based inhibition | Homo sapiens | |
1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one | the compound belongs to the ketobenzimidazoles, though containing a carbonyl moiety, that do not covalently modify Ser241. These inhibitors achieve potent inhibition of FAAH activity primarily from shape complementarity to the active site and through numerous hydrophobic interactions exhibiting excellent selectivity and good pharmacokinetic properties, nonmechanism-based inhibition. Pharmacokinetic parameters and selectivity 2, overview | Rattus norvegicus | |
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide | an irreversible covalent inhibitor, binding structure, overview | Homo sapiens | |
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide | an irreversible covalent inhibitor, binding structure, overview | Rattus norvegicus | |
OL-135 | 7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one | Homo sapiens | |
OL-135 | 7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one | Rattus norvegicus | |
URB597 | - |
Homo sapiens | |
URB597 | - |
Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | integral membrane protein | Rattus norvegicus | 16020 | - |
membrane | integral membrane protein | Homo sapiens | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O00519 | - |
- |
Rattus norvegicus | P97612 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged FAAH from Escherichia coli strain by nickel affinity chromatography | Rattus norvegicus |
recombinant His-tagged FAAH from Escherichia coli strain by nickel affinity chromatography | Homo sapiens |
Subunits | Comment | Organism |
---|---|---|
More | three major cavities in the active site are the membrane access channel, the acyl-chain binding pocket, and the cytosolic port, overview. The core structure of the FAAH monomer adopts an alpha/beta fold with a twisted 11-strand beta-sheet in the center and 24 alpha-helices surrounding the sheet | Rattus norvegicus |
More | three major cavities in the active site are the membrane access channel, the acyl-chain binding pocket, and the cytosolic port, overview. The core structure of the FAAH monomer adopts an alpha/beta fold with a twisted 11-strand beta-sheet in the center and 24 alpha-helices surrounding the sheet | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
FAAH | - |
Rattus norvegicus |
FAAH | - |
Homo sapiens |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.000003 | - |
pH and temperature not specified in the publication | Rattus norvegicus | URB597 | |
0.000004 | - |
pH and temperature not specified in the publication | Homo sapiens | URB597 | |
0.000005 | - |
pH and temperature not specified in the publication | Homo sapiens | 6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide | |
0.000016 | - |
pH and temperature not specified in the publication | Homo sapiens | OL-135 | |
0.000025 | - |
pH and temperature not specified in the publication | Rattus norvegicus | OL-135 | |
0.000028 | - |
pH and temperature not specified in the publication | Homo sapiens | 1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one | |
0.000036 | - |
pH and temperature not specified in the publication | Rattus norvegicus | 6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide | |
0.0001 | - |
pH and temperature not specified in the publication | Rattus norvegicus | 1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one |
General Information | Comment | Organism |
---|---|---|
evolution | fatty acid amide hydrolase is an amidase-signature family member | Rattus norvegicus |
evolution | fatty acid amide hydrolase is an amidase-signature family member | Homo sapiens |
additional information | catalytic triad is formed by Ser241-Ser217-Lys142 | Homo sapiens |
additional information | the active site is located in the center cavity defined by an atypical Ser-Ser-Lys catalytic triad which comprises the catalytic nucleophile residue Ser241 along with residues Ser217 and Lys142 | Rattus norvegicus |