| Reaction Details |
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 | Report a problem with these data |
| Target | Prothrombin |
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| Ligand | BDBM50111105 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEBML_208337 |
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| Ki | 0.005000±n/a nM |
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| Citation |  Lee, K; Jung, WH; Park, CW; Park, HD; Lee, SH; Kwon, OH Noncovalent tripeptidic thrombin inhibitors incorporating amidrazone, amine and amidine functions at P1. Bioorg Med Chem Lett12:1017-22 (2002) [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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| BDBM50111105 |
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| n/a |
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| Name | BDBM50111105 |
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| Synonyms: | (S)-1-((R)-2-Methanesulfonylamino-3,3-diphenyl-propionyl)-pyrrolidine-2-carboxylic acid (5-carbamimidoyl-thiophen-2-ylmethyl)-amide | 1-(2-Methanesulfonylamino-3,3-diphenyl-propionyl)-pyrrolidine-2-carboxylic acid (5-carbamimidoyl-thiophen-2-ylmethyl)-amide; compound with benzamidine | CHEMBL1795037 | CHEMBL7895 |
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| Type | Small organic molecule |
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| Emp. Form. | C27H31N5O4S2 |
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| Mol. Mass. | 553.696 |
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| SMILES | CS(=O)(=O)N[C@H](C(c1ccccc1)c1ccccc1)C(=O)N1CCC[C@H]1C(=O)NCc1ccc(s1)C(N)=N |
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| Structure | 
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