| Reaction Details |
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 | Report a problem with these data |
| Target | Coagulation factor X |
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| Ligand | BDBM17228 |
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| Substrate/Competitor | BDBM12658 |
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| Meas. Tech. | Enzyme Inhibition Assay |
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| pH | 7.5±n/a |
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| Temperature | 295.15±n/a K |
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| Ki | 0.82±n/a nM |
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| Citation |  Kochanny, MJ; Adler, M; Ewing, J; Griedel, BD; Ho, E; Karanjawala, R; Lee, W; Lentz, D; Liang, AM; Morrissey, MM; Phillips, GB; Post, J; Sacchi, KL; Sakata, ST; Subramanyam, B; Vergona, R; Walters, J; White, KA; Whitlow, M; Ye, B; Zhao, Z; Shaw, KJ Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa. Bioorg Med Chem15:2127-46 (2007) [PubMed] Article |
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| More Info.: | Get all data from this article, Inhibition_Run data, Solution Info, Assay Method |
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| Coagulation factor X |
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| Name: | Coagulation factor X |
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| Synonyms: | Activated coagulation factor X (FXa) | Activated factor Xa heavy chain | Coagulation factor X precursor | Coagulation factor Xa | F10 | FA10_HUMAN | Factor X heavy chain | Factor X light chain | Factor Xa | Stuart factor | Stuart-Prower factor |
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| Type: | Enzyme |
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| Mol. Mass.: | 54726.60 |
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| Organism: | Homo sapiens (Human) |
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| Description: | n/a |
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| Residue: | 488 |
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| Sequence: | MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEE
TCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKN
CELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERR
KRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQE
CKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGE
AVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGI
VSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSG
GPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPE
VITSSPLK
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| BDBM17228 |
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| BDBM12658 |
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| Name | BDBM17228 |
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| Synonyms: | N-{4-chloro-2-[(4-chlorophenyl)carbamoyl]phenyl}-3-methyl-1-benzothiophene-2-carboxamide | benzothiophene compound, 5 |
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| Type | Small organic molecule |
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| Emp. Form. | C23H16Cl2N2O2S |
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| Mol. Mass. | 455.356 |
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| SMILES | Cc1c(sc2ccccc12)C(=O)Nc1ccc(Cl)cc1C(=O)Nc1ccc(Cl)cc1 |
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| Structure | 
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