| Reaction Details |
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 | Report a problem with these data |
| Target | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit |
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| Ligand | BDBM42195 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | Counterscreen for inhibitors of PP5: fluorescence-based biochemical high throughput dose response assay for inhibitors of Protein Phosphatase 1 (PP1) |
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| IC50 | 67047±n/a nM |
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| Citation |  PubChem, PC Counterscreen for inhibitors of PP5: fluorescence-based biochemical high throughput dose response assay for inhibitors of Protein Phosphatase 1 (PP1) PubChem Bioassay(2010)[AID] |
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| More Info.: | Get all data from this article, Solution Info, Assay Method |
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| Serine/threonine-protein phosphatase PP1-alpha catalytic subunit |
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| Name: | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit |
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| Synonyms: | PP-1A | PP1A_HUMAN | PPP1A | PPP1CA | Serine/threonine protein phosphatase PP1-alpha catalytic subunit | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit | protein phosphatase 1, catalytic subunit, alpha isoform 3 |
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| Type: | PROTEIN |
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| Mol. Mass.: | 37510.66 |
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| Organism: | Homo sapiens (Human) |
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| Description: | ChEMBL_197827 |
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| Residue: | 330 |
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| Sequence: | MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK
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| BDBM42195 |
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| n/a |
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| Name | BDBM42195 |
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| Synonyms: | 2-Phenylamino-3-piperidin-1-yl-[1,4]naphthoquinone | 2-anilino-3-(1-piperidinyl)naphthalene-1,4-dione | 2-anilino-3-piperidin-1-ylnaphthalene-1,4-dione | 2-anilino-3-piperidino-1,4-naphthoquinone | 2-phenylazanyl-3-piperidin-1-yl-naphthalene-1,4-dione | MLS000528379 | SMR000120954 | cid_3147878 |
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| Type | Small organic molecule |
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| Emp. Form. | C21H20N2O2 |
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| Mol. Mass. | 332.3957 |
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| SMILES | O=C1C(Nc2ccccc2)=C(N2CCCCC2)C(=O)c2ccccc12 |t:10| |
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| Structure | 
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