Reaction Details |
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Target | Fatty-acid amide hydrolase 1 [30-579] |
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Ligand | BDBM50447745 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_1290134 (CHEMBL3117474) |
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IC50 | 0.340000±n/a nM |
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Citation | Kono, M; Matsumoto, T; Imaeda, T; Kawamura, T; Fujimoto, S; Kosugi, Y; Odani, T; Shimizu, Y; Matsui, H; Shimojo, M; Kori, M Design, synthesis, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase inhibitors. Bioorg Med Chem22:1468-78 (2014) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Fatty-acid amide hydrolase 1 [30-579] |
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Name: | Fatty-acid amide hydrolase 1 [30-579] |
Synonyms: | Anandamide amidohydrolase 1 | FAAH1_RAT | Faah | Faah1 | Fatty Acid Amide Hydrolase | Fatty Acid Amide Hydrolic, FAAH | Fatty-acid amide hydrolase (FAAH) | Fatty-acid amide hydrolase 1 | Fatty-acid amide hydrolase 1 (FAAH) | Fatty-acid amide hydrolase 1 (aa 30-579) | Oleamide hydrolase 1 |
Type: | Single-pass membrane protein; homodimer |
Mol. Mass.: | 60474.00 |
Organism: | Rattus norvegicus (rat) |
Description: | P97612 (aa 30-579) |
Residue: | 550 |
Sequence: | RWTGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKLQSG
ELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKG
HDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMLSFDCSNPLFGQTMNPWK
SSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGC
VYGQTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGY
YETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGRSFL
QNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSMRPRSAEKLWKLQH
EIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPV
TTVTAEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVE
QLMTPQKQPS
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BDBM50447745 |
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n/a |
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Name | BDBM50447745 |
Synonyms: | CHEMBL3113274 |
Type | Small organic molecule |
Emp. Form. | C19H17F2N7O |
Mol. Mass. | 397.3814 |
SMILES | Fc1cc(F)cc(c1)-c1ccnc(n1)N1CCN(CC1)C(=O)Nc1cccnn1 |
Structure |
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