| Reaction Details |
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 | Report a problem with these data |
| Target | ATP-sensitive inward rectifier potassium channel 1 |
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| Ligand | BDBM181712 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | Electrophysiology Assay |
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| pH | 7.4±n/a |
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| Temperature | 310.15±n/a K |
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| IC50 | 45±n/a nM |
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| Comments | extracted |
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| Citation |  Walsh, SP; Pasternak, A; DeJesus, RK; Tang, H; Pio, B; Shahripour, A; Belyk, KM; Chobanian, HR; Guo, Y; Frie, JL; Shi, Z; Chen, H; Blizzard, TA; Cato, B Inhibitors of the Renal Outer Medullary Potassium channel US Patent US9139585 Publication Date 9/22/2015 |
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| More Info.: | Get all data from this article, Assay Method |
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| ATP-sensitive inward rectifier potassium channel 1 |
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| Name: | ATP-sensitive inward rectifier potassium channel 1 |
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| Synonyms: | ATP-regulated potassium channel ROM-K | ATP-regulated potassium channel ROMK | ATP-sensitive inward rectifier potassium channel 1 | Egl nine homolog 1 | KCNJ1 | KCNJ1_HUMAN | Potassium channel (ATP modulatory) | Potassium inwardly-rectifying channel, subfamily J, member 1 | ROMK1 | Renal Outer Medullary Potassium (ROMK1) | The Renal Outer Medullary Potassium (ROMK) |
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| Type: | Enzyme Catalytic Domain |
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| Mol. Mass.: | 44809.08 |
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| Organism: | Homo sapiens (Human) |
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| Description: | gi_223460826 |
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| Residue: | 391 |
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| Sequence: | MNASSRNVFDTLIRVLTESMFKHLRKWVVTRFFGHSRQRARLVSKDGRCNIEFGNVEAQS
RFIFFVDIWTTVLDLKWRYKMTIFITAFLGSWFFFGLLWYAVAYIHKDLPEFHPSANHTP
CVENINGLTSAFLFSLETQVTIGYGFRCVTEQCATAIFLLIFQSILGVIINSFMCGAILA
KISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTVTPEGE
TIILDQININFVVDAGNENLFFISPLTIYHVIDHNSPFFHMAAETLLQQDFELVVFLDGT
VESTSATCQVRTSYVPEEVLWGYRFAPIVSKTKEGKYRVDFHNFSKTVEVETPHCAMCLY
NEKDVRARMKRGYDNPNFILSEVNETDDTKM
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| BDBM181712 |
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| n/a |
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| Name | BDBM181712 |
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| Synonyms: | US9139585, 7 |
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| Type | Small organic molecule |
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| Emp. Form. | C28H32N4O4 |
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| Mol. Mass. | 488.5781 |
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| SMILES | Cc1nc(ccc1C#N)C(O)CN1C2CCC1C1CCC2N1C[C@H](O)c1ccc2C(=O)OCc2c1C |r,TLB:19:20:12:14.15,18:17:12:14.15,11:12:21:19.18,THB:14:13:21:19.18,15:16:21:19.18,22:21:12:14.15| |
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| Structure | 
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