Reaction Details |
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Target | Dimer of Protein farnesyltransferase subunit beta |
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Ligand | BDBM50079088 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_51428 (CHEMBL664123) |
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IC50 | 9±n/a nM |
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Citation | Taveras, AG; Deskus, J; Chao, J; Vaccaro, CJ; Njoroge, FG; Vibulbhan, B; Pinto, P; Remiszewski, S; del Rosario, J; Doll, RJ; Alvarez, C; Lalwani, T; Mallams, AK; Rossman, RR; Afonso, A; Girijavallabhan, VM; Ganguly, AK; Pramanik, B; Heimark, L; Bishop, WR; Wang, L; Kirschmeier, P; James, L; Carr, D; Liu, M Identification of pharmacokinetically stable 3, 10-dibromo-8-chlorobenzocycloheptapyridine farnesyl protein transferase inhibitors with potent enzyme and cellular activities. J Med Chem42:2651-61 (1999) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Dimer of Protein farnesyltransferase subunit beta |
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Name: | Dimer of Protein farnesyltransferase subunit beta |
Synonyms: | Protein Farnesyltransferase (PFT) Chain B |
Type: | n/a |
Mol. Mass.: | n/a |
Description: | ASSAY_ID of EBI is 51428 |
Components: | This complex has 3 components. |
Component 1 |
Name: | Protein farnesyltransferase subunit beta |
Synonyms: | CAAX farnesyltransferase subunit alpha | CAAX farnesyltransferase subunit beta | FNTB | FNTB_HUMAN | FTase-alpha | FTase-beta | GGTase-I-alpha | Protein Farnesyltransferase (PFT) Chain B | Protein farnesyl/geranylgeranyl transferase | Protein farnesyltransferase beta subunit | Protein farnesyltransferase subunit beta | Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha | Ras proteins prenyltransferase subunit alpha | Ras proteins prenyltransferase subunit beta | Type I protein geranyl-geranyltransferase subunit alpha |
Type: | Enzyme Subunit |
Mol. Mass.: | 48766.02 |
Organism: | Homo sapiens (Human) |
Description: | Protein farnesyltransferase subunit beta |
Residue: | 437 |
Sequence: | MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS
SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY
LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG
GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY
SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF
YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV
PGFEELKDETSAEPATD
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Component 2 |
Name: | Protein farnesyltransferase subunit beta |
Synonyms: | CAAX farnesyltransferase subunit alpha | CAAX farnesyltransferase subunit beta | FNTB | FNTB_HUMAN | FTase-alpha | FTase-beta | GGTase-I-alpha | Protein Farnesyltransferase (PFT) Chain B | Protein farnesyl/geranylgeranyl transferase | Protein farnesyltransferase beta subunit | Protein farnesyltransferase subunit beta | Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha | Ras proteins prenyltransferase subunit alpha | Ras proteins prenyltransferase subunit beta | Type I protein geranyl-geranyltransferase subunit alpha |
Type: | Enzyme Subunit |
Mol. Mass.: | 48766.02 |
Organism: | Homo sapiens (Human) |
Description: | Protein farnesyltransferase subunit beta |
Residue: | 437 |
Sequence: | MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS
SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY
LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG
GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY
SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF
YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV
PGFEELKDETSAEPATD
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BDBM50079088 |
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n/a |
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Name | BDBM50079088 |
Synonyms: | 1-(4-{2-[4-((R)-3,10-Dibromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-piperidin-1-yl]-2-oxo-ethyl}-piperidin-1-yl)-2-pyrrol-1-yl-ethanone | CHEMBL91213 |
Type | Small organic molecule |
Emp. Form. | C32H35Br2ClN4O2 |
Mol. Mass. | 702.907 |
SMILES | Clc1cc(Br)c2[C@@H](C3CCN(CC3)C(=O)CC3CCN(CC3)C(=O)Cn3cccc3)c3ncc(Br)cc3CCc2c1 |
Structure |
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