| Reaction Details |
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 | Report a problem with these data |
| Target | Polyamine deacetylase HDAC10 |
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| Ligand | BDBM29589 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1590571 (CHEMBL3829040) |
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| IC50 | 4.5±n/a nM |
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| Citation |  Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L Development of Purine-Based Hydroxamic Acid Derivatives: Potent Histone Deacetylase Inhibitors with Marked in Vitro and in Vivo Antitumor Activities. J Med Chem59:5488-504 (2016) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Polyamine deacetylase HDAC10 |
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| Name: | Polyamine deacetylase HDAC10 |
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| Synonyms: | HD10 | HDA10_HUMAN | HDAC10 | Histone deacetylase | Histone deacetylase 10 | Human HDAC10 |
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| Type: | Chromatin regulator; hydrolase; repressor |
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| Mol. Mass.: | 71431.89 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Q969S8 |
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| Residue: | 669 |
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| Sequence: | MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEEL
GLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTG
AVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQ
YLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVA
AFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAV
LEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQ
DVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPD
ITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIA
ATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALS
MFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGL
AGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKM
LQCHPHLVA
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| BDBM29589 |
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| n/a |
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| Name | BDBM29589 |
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| Synonyms: | Faridak | LBH-589 | LBH-589B | Panobinostat | US10722597, Compound Panobinostat |
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| Type | Small organic molecule |
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| Emp. Form. | C21H23N3O2 |
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| Mol. Mass. | 349.4262 |
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| SMILES | Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 |
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| Structure | 
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