Reaction Details |
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Target | Fatty-acid amide hydrolase 1 [30-579] |
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Ligand | BDBM50244993 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_939361 (CHEMBL2327496) |
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IC50 | 3.8±n/a nM |
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Citation | Kono, M; Matsumoto, T; Kawamura, T; Nishimura, A; Kiyota, Y; Oki, H; Miyazaki, J; Igaki, S; Behnke, CA; Shimojo, M; Kori, M Synthesis, SAR study, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase (FAAH) inhibitors. Bioorg Med Chem21:28-41 (2012) [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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BDBM50244993 |
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n/a |
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Name | BDBM50244993 |
Synonyms: | 4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide | CHEMBL513553 |
Type | Small organic molecule |
Emp. Form. | C18H18N6OS |
Mol. Mass. | 366.44 |
SMILES | O=C(Nc1cccnc1)N1CCN(CC1)c1nc(ns1)-c1ccccc1 |
Structure |
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