Reaction Details |
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Target | Urokinase-type plasminogen activator |
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Ligand | BDBM14714 |
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Substrate/Competitor | BDBM14716 |
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Meas. Tech. | Serine Protease Inhibition Assay |
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pH | 7.8±n/a |
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Temperature | 295.15±n/a K |
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Ki | >3400±n/a nM |
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Citation | Olivero, AG; Eigenbrot, C; Goldsmith, R; Robarge, K; Artis, DR; Flygare, J; Rawson, T; Sutherlin, DP; Kadkhodayan, S; Beresini, M; Elliott, LO; DeGuzman, GG; Banner, DW; Ultsch, M; Marzec, U; Hanson, SR; Refino, C; Bunting, S; Kirchhofer, D A selective, slow binding inhibitor of factor VIIa binds to a nonstandard active site conformation and attenuates thrombus formation in vivo. J Biol Chem280:9160-9 (2005) [PubMed] Article |
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More Info.: | Get all data from this article, Solution Info, Assay Method |
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Urokinase-type plasminogen activator |
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Name: | Urokinase-type plasminogen activator |
Synonyms: | PLAU | U-plasminogen activator | UROK_HUMAN | Urokinase | Urokinase-type plasminogen activator (uPA) | Urokinase-type plasminogen activator/surface receptor |
Type: | Enzyme |
Mol. Mass.: | 48528.62 |
Organism: | Homo sapiens (Human) |
Description: | P00749 |
Residue: | 431 |
Sequence: | MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQ
HCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHN
YCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKII
GGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLG
RSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICL
PSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKML
CAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIR
SHTKEENGLAL
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BDBM14714 |
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BDBM14716 |
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Name | BDBM14714 |
Synonyms: | (2R)-N-[(3-aminobenzene)sulfonyl]-2-[(4-carbamimidoyl-3-hydroxyphenyl)amino]-2-(3,5-diethoxy-2-fluorophenyl)acetamide | G17905 | R-4-[2-(3-aminobenzenesulfonylamino)-1-(3,5-diethoxy-2-fluorophenyl)-2-oxoethylamino]-2-hydroxy-benzamidine.TFA |
Type | Small organic molecule |
Emp. Form. | C25H28FN5O6S |
Mol. Mass. | 545.583 |
SMILES | CCOc1cc(OCC)c(F)c(c1)[C@@H](Nc1ccc(C(N)=N)c(O)c1)C(=O)NS(=O)(=O)c1cccc(N)c1 |r| |
Structure |
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