| Reaction Details |
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 | Report a problem with these data |
| Target | Beta-secretase 2 |
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| Ligand | BDBM50259954 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEBML_1692053 |
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| IC50 | 1020±n/a nM |
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| Citation |  Butler, CR; Ogilvie, K; Martinez-Alsina, L; Barreiro, G; Beck, EM; Nolan, CE; Atchison, K; Benvenuti, E; Buzon, L; Doran, S; Gonzales, C; Helal, CJ; Hou, X; Hsu, MH; Johnson, EF; Lapham, K; Lanyon, L; Parris, K; O'Neill, BT; Riddell, D; Robshaw, A; Vajdos, F; Brodney, MA Aminomethyl-Derived Beta Secretase (BACE1) Inhibitors: Engaging Gly230 without an Anilide Functionality. J Med Chem60:386-402 (2017) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Beta-secretase 2 |
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| Name: | Beta-secretase 2 |
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| Synonyms: | AEPLC | ALP56 | ASP1 | ASP21 | Asp 1 | Aspartic-like protease 56 kDa | Aspartyl protease 1 | BACE2 | BACE2_HUMAN | Beta secretase 2 | Beta-secretase (BACE) | Beta-secretase 2 | Beta-secretase 2 (BACE-2) | Beta-secretase 2 precursor | Beta-site APP-cleaving enzyme 2 | Down region aspartic protease | Memapsin-1 | Membrane-associated aspartic protease 1 | beta-Secretase (BACE-2) |
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| Type: | Protein |
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| Mol. Mass.: | 56171.20 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Q9Y5Z0 |
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| Residue: | 518 |
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| Sequence: | MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGL
ALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAG
TPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATI
FESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVA
GSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKA
IVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISI
YLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFD
RAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCG
AILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK
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| BDBM50259954 |
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| n/a |
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| Name | BDBM50259954 |
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| Synonyms: | CHEMBL4094377 |
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| Type | Small organic molecule |
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| Emp. Form. | C16H20F5N3S |
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| Mol. Mass. | 381.407 |
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| SMILES | CC(C)(NCc1cc(c(F)cc1F)[C@]1(C)CCSC(N)=N1)C(F)(F)F |r,c:20| |
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| Structure | 
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