ChEMBL ligand: CHEMBL3655950
histone deacetylase 1/Histone deacetylase 1 in Human [ChEMBL: CHEMBL325] [GtoPdb: 2658] [UniProtKB: Q13547] There should be some charts here, you may need to enable JavaScript!
histone deacetylase 2/Histone deacetylase 2 in Human [ChEMBL: CHEMBL1937] [GtoPdb: 2616] [UniProtKB: Q92769] There should be some charts here, you may need to enable JavaScript!
histone deacetylase 3/Histone deacetylase 3 in Human [ChEMBL: CHEMBL1829] [GtoPdb: 2617] [UniProtKB: O15379] There should be some charts here, you may need to enable JavaScript!
histone deacetylase 6/Histone deacetylase 6 in Human [ChEMBL: CHEMBL1865] [GtoPdb: 2618] [UniProtKB: Q9UBN7] There should be some charts here, you may need to enable JavaScript!

DB	Assay description	Assay Type	Standard value	Standard parameter	Original value	Original units	Original parameter	Reference
histone deacetylase 1/Histone deacetylase 1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL325] [GtoPdb: 2658] [UniProtKB: Q13547]
ChEMBL	Enzyme Assay: Compounds for testing were diluted in DMSO to 50 fold the final concentration and a ten point three fold dilution series was made. The compounds were diluted in assay buffer (50 mM HEPES, pH 7.4, 100 mM KCl, 0.001% Tween-20, 0.05% BSA, 20 uM TCEP) to 6 fold their final concentration. The HDAC enzymes (purchased from BPS Biosciences) were diluted to 1.5 fold their final concentration in assay buffer. The tripeptide substrate and trypsin at 0.05 uM final concentration were diluted in assay buffer at 6 fold their final concentration. The final enzyme concentrations used in these assays were 3.3 ng/ml (HDAC1), 0.2 ng/ml (HDAC2), 0.08 ng/ml (HDAC3) and 2 ng/ml (HDAC6). The final substrate concentrations used were 16 uM (HDAC1), 10 uM (HDAC2), 17 uM (HDAC3) and 14 uM (HDAC6). Five ul of compounds and 20 ul of enzyme were added to wells of a black, opaque 384 well plate in duplicate. Enzyme and compound were incubated together at room temperature.	B	7.03	pIC50	94	nM	IC50	US-8614223-B2. Pyrimidine hydroxy amide compounds as protein deacetylase inhibitors and methods of use thereof (2013)
ChEMBL	Inhibition of HADC1 (unknown origin)	B	7.03	pIC50	94	nM	IC50	J Med Chem (2020) 63: 23-39 [PMID:31415174]
ChEMBL	Inhibition of HDAC1 (unknown origin)	B	7.03	pIC50	94	nM	IC50	J Med Chem (2022) 65: 12140-12162 [PMID:36073117]
ChEMBL	Inhibition of N-terminal GST-tagged HDAC1 (unknown origin) expressed in baculovirus expression system using FTS as substrate preincubated for 10 mins followed by substrate addition measured after 30 mins by enzymatic assay	B	7.03	pIC50	94	nM	IC50	Eur J Med Chem (2022) 229: 114090-114090 [PMID:34992037]
GtoPdb	-	-	7.03	pIC50	94	nM	IC50	Neuropsychopharmacology (2014) 39: 389-400 [PMID:23954848]
histone deacetylase 2/Histone deacetylase 2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1937] [GtoPdb: 2616] [UniProtKB: Q92769]
GtoPdb	-	-	6.89	pIC50	128	nM	IC50	Neuropsychopharmacology (2014) 39: 389-400 [PMID:23954848]
ChEMBL	Enzyme Assay: Compounds for testing were diluted in DMSO to 50 fold the final concentration and a ten point three fold dilution series was made. The compounds were diluted in assay buffer (50 mM HEPES, pH 7.4, 100 mM KCl, 0.001% Tween-20, 0.05% BSA, 20 uM TCEP) to 6 fold their final concentration. The HDAC enzymes (purchased from BPS Biosciences) were diluted to 1.5 fold their final concentration in assay buffer. The tripeptide substrate and trypsin at 0.05 uM final concentration were diluted in assay buffer at 6 fold their final concentration. The final enzyme concentrations used in these assays were 3.3 ng/ml (HDAC1), 0.2 ng/ml (HDAC2), 0.08 ng/ml (HDAC3) and 2 ng/ml (HDAC6). The final substrate concentrations used were 16 uM (HDAC1), 10 uM (HDAC2), 17 uM (HDAC3) and 14 uM (HDAC6). Five ul of compounds and 20 ul of enzyme were added to wells of a black, opaque 384 well plate in duplicate. Enzyme and compound were incubated together at room temperature.	B	6.89	pIC50	128	nM	IC50	US-8614223-B2. Pyrimidine hydroxy amide compounds as protein deacetylase inhibitors and methods of use thereof (2013)
ChEMBL	Inhibition of HDAC2 (unknown origin)	B	6.89	pIC50	128	nM	IC50	J Med Chem (2022) 65: 12140-12162 [PMID:36073117]
ChEMBL	Inhibition of N-terminal GST-tagged HDAC2 (unknown origin) expressed in baculovirus expression system using FTS as substrate preincubated for 10 mins followed by substrate addition measured after 30 mins by enzymatic assay	B	6.89	pIC50	128	nM	IC50	Eur J Med Chem (2022) 229: 114090-114090 [PMID:34992037]
histone deacetylase 3/Histone deacetylase 3 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1829] [GtoPdb: 2617] [UniProtKB: O15379]
ChEMBL	Enzyme Assay: Compounds for testing were diluted in DMSO to 50 fold the final concentration and a ten point three fold dilution series was made. The compounds were diluted in assay buffer (50 mM HEPES, pH 7.4, 100 mM KCl, 0.001% Tween-20, 0.05% BSA, 20 uM TCEP) to 6 fold their final concentration. The HDAC enzymes (purchased from BPS Biosciences) were diluted to 1.5 fold their final concentration in assay buffer. The tripeptide substrate and trypsin at 0.05 uM final concentration were diluted in assay buffer at 6 fold their final concentration. The final enzyme concentrations used in these assays were 3.3 ng/ml (HDAC1), 0.2 ng/ml (HDAC2), 0.08 ng/ml (HDAC3) and 2 ng/ml (HDAC6). The final substrate concentrations used were 16 uM (HDAC1), 10 uM (HDAC2), 17 uM (HDAC3) and 14 uM (HDAC6). Five ul of compounds and 20 ul of enzyme were added to wells of a black, opaque 384 well plate in duplicate. Enzyme and compound were incubated together at room temperature.	B	6.66	pIC50	219	nM	IC50	US-8614223-B2. Pyrimidine hydroxy amide compounds as protein deacetylase inhibitors and methods of use thereof (2013)
GtoPdb	-	-	6.66	pIC50	218	nM	IC50	Neuropsychopharmacology (2014) 39: 389-400 [PMID:23954848]
ChEMBL	Inhibition of HDAC3 (unknown origin)	B	6.66	pIC50	218	nM	IC50	J Med Chem (2022) 65: 12140-12162 [PMID:36073117]
ChEMBL	Inhibition of N-terminal GST-tagged HDAC3 (unknown origin) expressed in baculovirus expression system using FTS as substrate preincubated for 10 mins followed by substrate addition measured after 30 mins by enzymatic assay	B	6.66	pIC50	218	nM	IC50	Eur J Med Chem (2022) 229: 114090-114090 [PMID:34992037]
histone deacetylase 6/Histone deacetylase 6 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1865] [GtoPdb: 2618] [UniProtKB: Q9UBN7]
ChEMBL	Inhibition of heat inactivated recombinant human HDAC6 expressed in HEK293T cells assessed as inhibition of tau protein deacetylation incubated for 16 hrs by immunoblot analysis	B	8.7	pIC50	2	nM	IC50	Eur J Med Chem (2021) 209: 112915-112915 [PMID:33139110]
ChEMBL	Inhibition of recombinant full length human N-terminal GST-tagged HDAC6 expressed in baculovirus infected sf9 insect cells pretreated with compound followed by Fluor de Lys deacetylase substrate addition by fluorescence method	B	8.7	pIC50	2	nM	IC50	J Med Chem (2019) 62: 10711-10739 [PMID:31710483]
ChEMBL	Enzyme Assay: Compounds for testing were diluted in DMSO to 50 fold the final concentration and a ten point three fold dilution series was made. The compounds were diluted in assay buffer (50 mM HEPES, pH 7.4, 100 mM KCl, 0.001% Tween-20, 0.05% BSA, 20 uM TCEP) to 6 fold their final concentration. The HDAC enzymes (purchased from BPS Biosciences) were diluted to 1.5 fold their final concentration in assay buffer. The tripeptide substrate and trypsin at 0.05 uM final concentration were diluted in assay buffer at 6 fold their final concentration. The final enzyme concentrations used in these assays were 3.3 ng/ml (HDAC1), 0.2 ng/ml (HDAC2), 0.08 ng/ml (HDAC3) and 2 ng/ml (HDAC6). The final substrate concentrations used were 16 uM (HDAC1), 10 uM (HDAC2), 17 uM (HDAC3) and 14 uM (HDAC6). Five ul of compounds and 20 ul of enzyme were added to wells of a black, opaque 384 well plate in duplicate. Enzyme and compound were incubated together at room temperature.	B	8.7	pIC50	2	nM	IC50	US-8614223-B2. Pyrimidine hydroxy amide compounds as protein deacetylase inhibitors and methods of use thereof (2013)
ChEMBL	Inhibition of HDAC6 (unknown origin)	B	8.77	pIC50	1.7	nM	IC50	Bioorg Med Chem Lett (2021) 47: 128204-128204 [PMID:34139324]
ChEMBL	Inhibition of HDAC6 (unknown origin)	B	8.77	pIC50	1.7	nM	IC50	J Med Chem (2022) 65: 12140-12162 [PMID:36073117]
ChEMBL	Inhibition of N-terminal GST-tagged HDAC6 (unknown origin) expressed in baculovirus expression system using FTS as substrate preincubated for 10 mins followed by substrate addition measured after 30 mins by enzymatic assay	B	8.77	pIC50	1.7	nM	IC50	Eur J Med Chem (2022) 229: 114090-114090 [PMID:34992037]
ChEMBL	Inhibition of HDAC6 (unknown origin)	B	8.77	pIC50	1.7	nM	IC50	Eur J Med Chem (2021) 226: 113874-113874 [PMID:34619465]
ChEMBL	Inhibition of HADC6 (unknown origin)	B	8.77	pIC50	1.7	nM	IC50	J Med Chem (2020) 63: 23-39 [PMID:31415174]
ChEMBL	Inhibition of N-terminal GST-tagged full-length human HDAC6 expressed in Sf9 infected baculovirus system using FTS as substrate preincubated for 10 mins followed by substrate addition and measured for 30 mins	B	8.77	pIC50	1.7	nM	IC50	Eur J Med Chem (2021) 218: 113383-113383 [PMID:33799069]
GtoPdb	-	-	8.77	pIC50	1.7	nM	IC50	Neuropsychopharmacology (2014) 39: 389-400 [PMID:23954848]

ChEMBL data shown on this page come from version 34:

Zdrazil B, Felix E, Hunter F, Manners EJ, Blackshaw J, Corbett S, de Veij M, Ioannidis H, Lopez DM, Mosquera JF, Magarinos MP, Bosc N, Arcila R, Kizilören T, Gaulton A, Bento AP, Adasme MF, Monecke P, Landrum GA, Leach AR. (2024). The ChEMBL Database in 2023: a drug discovery platform spanning multiple bioactivity data types and time periods. Nucleic Acids Res., 52(D1). DOI: 10.1093/nar/gkad1004. [EPMCID:10767899] [PMID:37933841]
Davies M, Nowotka M, Papadatos G, Dedman N, Gaulton A, Atkinson F, Bellis L, Overington JP. (2015) 'ChEMBL web services: streamlining access to drug discovery data and utilities.' Nucleic Acids Res., 43(W1). DOI: 10.1093/nar/gkv352. [EPMCID:25883136]