ChEMBL ligand: CHEMBL3629569
indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Human [ChEMBL: CHEMBL4685] [GtoPdb: 2829] [UniProtKB: P14902] There should be some charts here, you may need to enable JavaScript!
tryptophan 2,3-dioxygenase/Tryptophan 2,3-dioxygenase in Human [ChEMBL: CHEMBL2140] [GtoPdb: 2887] [UniProtKB: P48775] 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
indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4685] [GtoPdb: 2829] [UniProtKB: P14902]
ChEMBL	Binding affinity to NT647 dye labeled recombinant human IDO1 (1 to 403 residues) by microscale thermophoresis method	B	5.48	pKd	3300	nM	Kd	Eur J Med Chem (2017) 141: 169-177 [PMID:29031064]
ChEMBL	Inhibition of IDO1 (unknown origin) by in-vitro assay	B	8.14	pKi	7.2	nM	Ki	Eur J Med Chem (2017) 140: 293-304 [PMID:28963992]
ChEMBL	Inhibition of IDO1 (unknown origin)	B	8.15	pKi	7	nM	Ki	Medchemcomm (2017) 8: 1378-1392 [PMID:30108849]
GtoPdb	-	-	8.24	pKi	5.8	nM	Ki	J Med Chem (2019) 62: 6705-6733 [PMID:31264862]
ChEMBL	Inhibition of human IDO1	B	6	pIC50	<1000	nM	IC50	J Med Chem (2015) 58: 8762-8782 [PMID:26207924]
ChEMBL	Inhibition of C-terminal 6His-tagged human IDO using L-tryptophan as substrate preincubated for 5 mins followed by substrate addition measured after 15 mins by spectrophotometric analysis	B	6	pIC50	<1000	nM	IC50	J Med Chem (2015) 58: 9421-9437 [PMID:25970480]
ChEMBL	Inhibition of recombinant human IDO1 assessed as L-kynurenine release preincubated for 5 mins followed by addition of L-tryptophan for 15 mins by spectrophotometer	B	6	pIC50	<1000	nM	IC50	Medchemcomm (2016) 7: 409-419
ChEMBL	Enzymatic IDO Assay: The IC50 values for each compound were determined by testing the activity of IDO in a mixture containing 50 mM potassium phosphate buffer at pH 6.5; 70 nM purified human IDO protein, 200 μM L-tryptophan, 20 mM ascorbate, 20 μM methylene blue, 0.1% DMSO. The inhibitors were initially diluted in DMSO at 100 mM and were diluted in potassium phosphate 50 mM, added to the reaction mixture at final concentrations raging from 1 mM to 5 nM and preincubated with the enzyme for 5 min at 25° C. The reaction was started by addition of L-tryptophan to 200 μM and incubated 15 min at 37° C. The reaction was stopped by addition of 0.5 vol of 30% trichloroacetic acid and incubated 30 min at 60° C. to hydrolyze N-formylkynurenine to kynurenine. The reaction was centrifuged at 3400 g for 5 min to remove precipitated protein and the supernatant was reacted with 2% (w/v) of p-dimethylaminobenzaldehyde in acetic acid. The reaction was incubated 10 min at 25° C. and read at 480 nm in a spectrophotometer. Control samples with no IDO inhibitor, or with no IDO enzyme or with the reference inhibitors 1-methyl-tryptophan (200 μM) and menadione (1.2 μM) were used as controls to set the parameters for the non-linear regressions necessary for determination of the IC50 for each compound. Nonlinear regressions and determination of the IC50 values were performed using the GraphPad Prism 4 software. Compounds with an IC50 of less than 500 μM were considered as active inhibitors in this assay.	B	6	pIC50	<1000	nM	IC50	US-10233190-B2. IDO inhibitors (2019)
ChEMBL	Inhibition of full length recombinant human His-tagged IDO1 expressed in mouse LLTC cells using L-tryptophan as substrate after 24 hrs	B	6.23	pIC50	590	nM	IC50	Eur J Med Chem (2017) 126: 983-996 [PMID:28011425]
ChEMBL	Inhibition of IFNgamma-induced IDO1 in human HeLa cells using L-tryptophan as substrate after 24 hrs	B	6.39	pIC50	410	nM	IC50	Eur J Med Chem (2017) 138: 199-211 [PMID:28667875]
ChEMBL	Inhibition of IDO1 in IFN-gamma stimulated human HeLa cells assessed as reduction in kynurenine production using L-tryptophan as substrate incubated for 24 hrs	B	6.72	pIC50	190	nM	IC50	Eur J Med Chem (2019) 184: 111750-111750 [PMID:31610376]
ChEMBL	Inhibition of recombinant human IDO1 S167A mutant expressed in Escherichia coli SG13009(pREP4) using L-Tryptophan as substrate after 25 mins by fluorescence assay	B	6.89	pIC50	130	nM	IC50	Eur J Med Chem (2017) 126: 983-996 [PMID:28011425]
ChEMBL	Inhibition of recombinant human IDO1 expressed in Escherichia coli EC538 assessed as reduction in N-formylkynurenine formation using L-tryptophan as substrate incubated for 30 mins by methylene blue reagent based concurrent assay	B	6.96	pIC50	110	nM	IC50	Bioorg Med Chem (2021) 39: 116160-116160 [PMID:33901770]
ChEMBL	Inhibition of recombinant human IDO1 expressed in Escherichia coli EC538 assessed as reduction in N-formylkynurenine formation using L-tryptophan as substrate incubated for 30 mins by methylene blue reagent based assay	B	7.1	pIC50	80	nM	IC50	Bioorg Med Chem (2021) 39: 116160-116160 [PMID:33901770]
ChEMBL	Inhibition of purified human IDO1 using L-tryptophan as substrate preincubated for 5 mins followed by substrate addition and measured after 15 mins by spectrophotometric method	B	7.22	pIC50	60	nM	IC50	J Med Chem (2019) 62: 6705-6733 [PMID:31264862]
ChEMBL	Inhibition of recombinant human IDO1 expressed in bacterial expression system using L-Tryptophan as substrate after 25 mins in absence of GSH and presence of tween20 by fluorescence assay	B	7.22	pIC50	60	nM	IC50	Eur J Med Chem (2017) 126: 983-996 [PMID:28011425]
ChEMBL	Inhibition of recombinant human IDO1 assessed as reduction in N-formylkynurenine formation using L-tryptophan as substrate incubated for 45 mins by methylene blue reagent based assay	B	7.3	pIC50	50	nM	IC50	Bioorg Med Chem (2021) 39: 116160-116160 [PMID:33901770]
ChEMBL	Inhibition of recombinant human IDO1 assessed as conversion of N-formylkynurenine to kynurenine incubated for 1 hr by fluorescence analysis	B	7.42	pIC50	38	nM	IC50	J Med Chem (2016) 59: 282-293 [PMID:26642377]
ChEMBL	Inhibition of IDO1 (unknown origin)	B	7.55	pIC50	28	nM	IC50	Medchemcomm (2016) 7: 409-419
ChEMBL	Inhibition of recombinant human IDO1 expressed in T-REx-293 cells assessed as reduction in kynurenine level measured after 16 hrs	B	7.08	pEC50	83	nM	EC50	J Med Chem (2019) 62: 6705-6733 [PMID:31264862]
ChEMBL	Inhibition of IDO1 (unknown origin) by cell based assay	B	7.12	pEC50	75	nM	EC50	Eur J Med Chem (2017) 140: 293-304 [PMID:28963992]
ChEMBL	Inhibition of IDO1 (unknown origin) by cell based assay	B	7.12	pEC50	75	nM	EC50	Medchemcomm (2017) 8: 1378-1392 [PMID:30108849]
ChEMBL	Inhibition of IDO1 in IFNgamma-stimulated human HeLa cells incubated for 24 hrs	B	7.21	pEC50	61	nM	EC50	J Med Chem (2016) 59: 282-293 [PMID:26642377]
tryptophan 2,3-dioxygenase/Tryptophan 2,3-dioxygenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2140] [GtoPdb: 2887] [UniProtKB: P48775]
GtoPdb	-	-	6	pIC50	<1000	nM	IC50	J Med Chem (2015) 58: 8762-82 [PMID:26207924]
ChEMBL	Inhibition of TDO (unknown origin)	B	6	pIC50	<1000	nM	IC50	J Med Chem (2015) 58: 8762-8782 [PMID:26207924]
ChEMBL	TDO Coupled Biochemical Assays: In two separate assays, 2.5 μg/μl of human TDO protein was pre-incubated for 10 minutes at RT with test compounds 680C91 and LM10 in the presence of 50 mM KH2PO4, pH 7.0, 0.5 mM EDTA, 0.5 mM EGTA, 0.05% Triton X-100, 20 mM ascorbate, 500 U/ml catalase, 10 μM methylene blue at RT in a 384 well plate. 0.05 μg/μl kynurenine formamidase (drosophila) and 330 μM L-tryptophan were added and the assays were incubated at room temperature (RT) for 17 min. Assays were stopped and the level of kynurenine was determined by incubation with Ehrlich's reagent to a final concentration of 1.33% at RT for 5 min. Fluorescence intensity was read at 475 nm/530 nm.	B	6.3	pIC50	501	nM	IC50	US-10155972-B2. Screening method (2018)
ChEMBL	Inhibition of recombinant human TDO2 expressed in Escherichia coli BL21 (DE3) assessed as reduction in N-formylkynurenine formation using L-tryptophan as substrate incubated for 30 mins by methylene blue reagent based concurrent assay	B	6.82	pIC50	150	nM	IC50	Bioorg Med Chem (2021) 39: 116160-116160 [PMID:33901770]
ChEMBL	Inhibition of recombinant human TDO2 expressed in Escherichia coli BL21 (DE3) assessed as reduction in N-formylkynurenine formation using L-tryptophan as substrate incubated for 30 mins by methylene blue reagent based assay	B	7.52	pIC50	30	nM	IC50	Bioorg Med Chem (2021) 39: 116160-116160 [PMID:33901770]

ChEMBL data shown on this page come from version 36:

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]