| Reaction Details |
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 | Report a problem with these data |
| Target | Prothrombin |
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| Ligand | BDBM50107476 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEBML_207982 |
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| IC50 | 1400±n/a nM |
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| Citation |  Das, J; Kimball, SD; Hall, SE; Han, WC; Iwanowicz, E; Lin, J; Moquin, RV; Reid, JA; Sack, JS; Malley, MF; Chang, CY; Chong, S; Wang-Iverson, DB; Roberts, DG; Seiler, SM; Schumacher, WA; Ogletree, ML Molecular design and structure--activity relationships leading to the potent, selective, and orally active thrombin active site inhibitor BMS-189664. Bioorg Med Chem Lett12:45-9 (2001) [PubMed] |
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| More Info.: | Get all data from this article, Assay Method |
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| Prothrombin |
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| Name: | Prothrombin |
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| Synonyms: | Activation peptide fragment 1 | Activation peptide fragment 2 | Coagulation factor II | F2 | Prothrombin precursor | THRB_HUMAN | Thrombin heavy chain | Thrombin light chain |
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| Type: | Protein |
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| Mol. Mass.: | 70029.57 |
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| Organism: | Homo sapiens (Human) |
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| Description: | P00734 |
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| Residue: | 622 |
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| Sequence: | MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC
VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV
NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE
CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA
QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG
DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI
DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN
DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP
VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST
RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGE
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| BDBM50107476 |
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| n/a |
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| Name | BDBM50107476 |
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| Synonyms: | 1-[(S)-2-((S)-Naphthalene-2-sulfonylamino)-3-phenyl-propionyl]-pyrrolidine-2-carboxylic acid (4-guanidino-butyl)-amide | CHEMBL428818 |
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| Type | Small organic molecule |
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| Emp. Form. | C29H36N6O4S |
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| Mol. Mass. | 564.699 |
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| SMILES | NC(=N)NCCCCNC(=O)[C@@H]1CCCN1C(=O)[C@@H](Cc1ccccc1)NS(=O)(=O)c1ccc2ccccc2c1 |
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| Structure | 
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