Reaction Details |
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Target | Prolyl endopeptidase FAP |
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Ligand | BDBM50326392 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_1335495 (CHEMBL3239280) |
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IC50 | 17±n/a nM |
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Citation | Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P Extended structure-activity relationship and pharmacokinetic investigation of (4-quinolinoyl)glycyl-2-cyanopyrrolidine inhibitors of fibroblast activation protein (FAP). J Med Chem57:3053-74 (2014) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Prolyl endopeptidase FAP |
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Name: | Prolyl endopeptidase FAP |
Synonyms: | Fap | Fibroblast activation protein (FAP) | SEPR_MOUSE | Seprase |
Type: | Enzyme |
Mol. Mass.: | 87949.14 |
Organism: | Mus musculus (Mouse) |
Description: | P97321 |
Residue: | 761 |
Sequence: | MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPN
WISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSK
LWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPP
FQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYG
DGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVS
SERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQD
ATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPG
RRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGR
TDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQV
YGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQ
LTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIY
SERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNA
QVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD
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BDBM50326392 |
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n/a |
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Name | BDBM50326392 |
Synonyms: | (2S)-1-({(2S,4S)-4-[2-(1,3-Dihydro-2H-isoindol-2-yl)-2-oxoethyl]-5-oxopyrrolidin-2-yl}carbonyl)-4,4-difluoropyrrolidine-2-carbonitrile | CHEMBL1243153 |
Type | Small organic molecule |
Emp. Form. | C20H20F2N4O3 |
Mol. Mass. | 402.3946 |
SMILES | FC1(F)C[C@@H](C#N)N(C1)C(=O)[C@@H]1C[C@@H](CC(=O)N2Cc3ccccc3C2)C(=O)N1 |r| |
Structure |
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