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ChEMBL ligand: CHEMBL2207503 (CCT-241736, CCT241736, Ep-0042, Ep0042) |
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DB | Assay description | Assay Type | Standard value | Standard parameter | Original value | Original units | Original parameter | Reference |
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CYP1A2/Cytochrome P450 1A2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3356] [GtoPdb: 1319] [UniProtKB: P05177] | ||||||||
ChEMBL | Inhibition Assays: Inhibition of CYP isozymes was determined using a mixture of probe substrates. The samples were incubated for 10 minutes followed by protein precipitation with methanol. The substrate metabolites in each sample were measured by LC/MS/MS using reverse-phase liquid chromatography and positive ion mode ESI with multiple reaction monitoring (MRM). | B | 4.3 | pIC50 | >50000 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
CYP2A6/Cytochrome P450 2A6 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5282] [GtoPdb: 1321] [UniProtKB: P11509] | ||||||||
ChEMBL | Inhibition Assays: Inhibition of CYP isozymes was determined using a mixture of probe substrates. The samples were incubated for 10 minutes followed by protein precipitation with methanol. The substrate metabolites in each sample were measured by LC/MS/MS using reverse-phase liquid chromatography and positive ion mode ESI with multiple reaction monitoring (MRM). | B | 4.3 | pIC50 | >50000 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
CYP2C19/Cytochrome P450 2C19 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3622] [GtoPdb: 1328] [UniProtKB: P33261] | ||||||||
ChEMBL | Inhibition Assays: Inhibition of CYP isozymes was determined using a mixture of probe substrates. The samples were incubated for 10 minutes followed by protein precipitation with methanol. The substrate metabolites in each sample were measured by LC/MS/MS using reverse-phase liquid chromatography and positive ion mode ESI with multiple reaction monitoring (MRM). | B | 7.52 | pIC50 | 30 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
CYP2C9/Cytochrome P450 2C9 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3397] [GtoPdb: 1326] [UniProtKB: P11712] | ||||||||
ChEMBL | Inhibition Assays: Inhibition of CYP isozymes was determined using a mixture of probe substrates. The samples were incubated for 10 minutes followed by protein precipitation with methanol. The substrate metabolites in each sample were measured by LC/MS/MS using reverse-phase liquid chromatography and positive ion mode ESI with multiple reaction monitoring (MRM). | B | 7.52 | pIC50 | 30 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
CYP2D6/Cytochrome P450 2D6 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL289] [GtoPdb: 1329] [UniProtKB: P10635] | ||||||||
ChEMBL | Inhibition Assays: Inhibition of CYP isozymes was determined using a mixture of probe substrates. The samples were incubated for 10 minutes followed by protein precipitation with methanol. The substrate metabolites in each sample were measured by LC/MS/MS using reverse-phase liquid chromatography and positive ion mode ESI with multiple reaction monitoring (MRM). | B | 7.52 | pIC50 | 30 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
CYP3A4/Cytochrome P450 3A4 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL340] [GtoPdb: 1337] [UniProtKB: P08684] | ||||||||
ChEMBL | Inhibition Assays: Inhibition of CYP isozymes was determined using a mixture of probe substrates. The samples were incubated for 10 minutes followed by protein precipitation with methanol. The substrate metabolites in each sample were measured by LC/MS/MS using reverse-phase liquid chromatography and positive ion mode ESI with multiple reaction monitoring (MRM). | B | 4.3 | pIC50 | >50000 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
Kv11.1/HERG in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL240] [GtoPdb: 572] [UniProtKB: Q12809] | ||||||||
ChEMBL | Inhibition of human ERG by whole-cell voltage clamping | B | 4.6 | pIC50 | >25000 | nM | IC50 | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | Cell-Based Electrophysiology Assays: All hERG percentage inhibitions at 10 uM compound concentration were determined by Millipore in a high-throughput cell-based electrophysiology assay for inhibition of hERG tail current41, and values are reported as a mean of multiple determinations. 0.3% DMSO aqueous vehicle negative control gave 7-16% inhibition. Cisapride (1 uM) positive control gave 96-104% inhibition. All hERG IC50 values were determined by Millipore,41 and the hERG IC50 for Example 1 was also determined by Cyprotex plc measuring hERG tail-currents by whole-cell voltage-clamping. | B | 4.6 | pIC50 | >25000 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
aurora kinase A/Serine/threonine-protein kinase Aurora-A in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4722] [GtoPdb: 1936] [UniProtKB: O14965] | ||||||||
GtoPdb | - | - | 8.01 | pKd | 9.8 | nM | Kd | Eur J Pharm Sci (2019) 139: 104899 [PMID:30953752] |
ChEMBL | Binding affinity to Aurora A kinase | B | 8.12 | pKd | 7.5 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 8.12 | pKd | 7.5 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Binding affinity to Aurora A (unknown origin) assessed as dissociation constant | B | 8.12 | pKd | 7.5 | nM | Kd | J Med Chem (2021) 64: 2878-2900 [PMID:33719439] |
ChEMBL | Inhibition of GST-tagged human Aurora A kinase expressed in baculovirus system | B | 7.42 | pIC50 | 38 | nM | IC50 | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | Aurora Kinase Assays: Myc-tagged Aurora A was transfected in Hela cells using Lipofectamine LTX in 24 well plates, and 24 hours after transfection, cells were treated with different concentrations of Example 1 for 2 hours. Cells were then lysed in 2×LDS sample buffer. Proteins from different samples were resolved by 4-12% Bis-Tris NuPage (Invitrogen) gels and analysed by western blotting using P-histone H3 (S10) and P-Aurora A (T288) antibodies. | B | 7.42 | pIC50 | 38 | nM | IC50 | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Inhibition of Aurora A kinase autophosphorylation at T288 in human HeLa cells | B | 7.52 | pIC50 | 30 | nM | IC50 | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
aurora kinase B/Serine/threonine-protein kinase Aurora-B in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2185] [GtoPdb: 1937] [UniProtKB: Q96GD4] | ||||||||
GtoPdb | - | - | 7.19 | pKd | 64 | nM | Kd | Eur J Pharm Sci (2019) 139: 104899 [PMID:30953752] |
ChEMBL | Binding affinity to Aurora B kinase | B | 7.32 | pKd | 48 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 7.32 | pKd | 48 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Binding affinity to Aurora B (unknown origin) assessed as dissociation constant | B | 7.32 | pKd | 48 | nM | Kd | J Med Chem (2021) 64: 2878-2900 [PMID:33719439] |
ChEMBL | Inhibition of Aurora B kinase-mediated Histone H3 phosphorylation at S10 in human HeLa cells | B | 6.83 | pIC50 | 148 | nM | IC50 | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
fms related receptor tyrosine kinase 3/Tyrosine-protein kinase receptor FLT3 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1974] [GtoPdb: 1807] [UniProtKB: P36888] | ||||||||
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 6.96 | pKd | 110 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Binding affinity to FLT3 R834Q mutant | B | 6.96 | pKd | 110 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
GtoPdb | Affinity for FLT3-ITD mutant | - | 7.47 | pKd | 34 | nM | Kd | Eur J Pharm Sci (2019) 139: 104899 [PMID:30953752] |
GtoPdb | Affinity for WT FLT3 | - | 7.59 | pKd | 26 | nM | Kd | Eur J Pharm Sci (2019) 139: 104899 [PMID:30953752] |
ChEMBL | Binding affinity to FLT3 N841I mutant | B | 7.8 | pKd | 16 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 7.8 | pKd | 16 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 7.85 | pKd | 14 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Binding affinity to FLT3 D835Y mutant | B | 7.85 | pKd | 14 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 7.96 | pKd | 11 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Binding affinity to FLT3 D835H mutant | B | 7.96 | pKd | 11 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | Binding affinity to FLT3 (unknown origin) assessed as dissociation constant | B | 8.21 | pKd | 6.2 | nM | Kd | J Med Chem (2021) 64: 2878-2900 [PMID:33719439] |
ChEMBL | Binding affinity to FLT3 | B | 8.21 | pKd | 6.2 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 8.21 | pKd | 6.2 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | KINOMEScan Technology Assays: The kinase selectivity was assessed by profiling Example 1 in a 442-kinase panel (386 non-mutant kinases) at a concentration of 1 μM using the KINOMEScan™ technology.28 The S(10) selectivity score that is calculated by dividing the number of non-mutant kinases for which >90% competition was observed in the assay (this is measured as <10% of control) by the total number of non-mutant kinases tested, was determined as 0.057, i.e. 22 hits from the 386 non-mutant kinases tested. Aurora-A, -B, and -C were potently inhibited with % control values determined as 3.4%, 1%, and 16% respectively. | B | 8.29 | pKd | 5.1 | nM | Kd | US-9447092-B2. Pharmaceutically active compounds (2016) |
ChEMBL | Binding affinity to FLT3 K663Q mutant | B | 8.29 | pKd | 5.1 | nM | Kd | J Med Chem (2012) 55: 8721-8734 [PMID:23043539] |
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]