ChEMBL ligand: CHEMBL1812545
indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Human [ChEMBL: CHEMBL4685] [GtoPdb: 2829] [UniProtKB: P14902] indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Mouse [ChEMBL: CHEMBL1075294] [GtoPdb: 2829] [UniProtKB: P28776] 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] tryptophan 2,3-dioxygenase/Tryptophan 2,3-dioxygenase in Mouse [ChEMBL: CHEMBL1075307] [GtoPdb: 2887] [UniProtKB: P48776] 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	Inhibition of human IDO1 transfected in mouse P815B clone-6 cells by HPLC analysis	B	4	pIC50	>100000	nM	IC50	J Med Chem (2012) 55: 5270-5290 [PMID:22616902]
indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Mouse (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1075294] [GtoPdb: 2829] [UniProtKB: P28776]
ChEMBL	Inhibition of mouse IDO1 in P815 clone 6 cells by HPLC analysis	B	4	pIC50	>100000	nM	IC50	J Med Chem (2012) 55: 5270-5290 [PMID:22616902]
tryptophan 2,3-dioxygenase/Tryptophan 2,3-dioxygenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2140] [GtoPdb: 2887] [UniProtKB: P48775]
ChEMBL	Uncompetitive inhibition of recombinant full length C-terminal His-tagged human TDO expressed in Escherichia coli using L-Trp as substrate after 30 mins by Dixon plot analysis	B	5.13	pKi	7470	nM	Ki	Eur J Med Chem (2018) 160: 133-145 [PMID:30321802]
GtoPdb	-	-	5.25	pKi	5600	nM	Ki	Proc Natl Acad Sci USA (2012) 109: 2497-502 [PMID:22308364]; J Med Chem (2011) 54: 5320-34 [PMID:21726069]
ChEMBL	Competitive inhibition of human recombinant TDO expressed in Escherichia coli BL21 using L-tryptophan as substrate by measuring conversion of N-formylkynurenine into kynurenine after 30 mins by Michaelis-Menten steady state analysis	B	5.25	pKi	5600	nM	Ki	J Med Chem (2011) 54: 5320-5334 [PMID:21726069]
ChEMBL	Inhibition of recombinant human TDO expressed in Escherichia coli using L-Trp as substrate after 10 to 60 mins	B	5.25	pKi	5600	nM	Ki	Eur J Med Chem (2018) 160: 133-145 [PMID:30321802]
ChEMBL	Inhibition of TDO (unknown origin)	B	5.26	pKi	5500	nM	Ki	Bioorg Med Chem (2019) 27: 1087-1098 [PMID:30773421]
ChEMBL	Inhibition of human TDO transfected in mouse P815B clone 19 cells by HPLC analysis	B	4.55	pIC50	28000	nM	IC50	J Med Chem (2012) 55: 5270-5290 [PMID:22616902]
ChEMBL	Inhibition of recombinant full length C-terminal His-tagged human TDO expressed in Escherichia coli using L-Trp as substrate after 30 mins	B	4.73	pIC50	18700	nM	IC50	Eur J Med Chem (2018) 160: 133-145 [PMID:30321802]
ChEMBL	Inhibition of recombinant human TDO expressed in Escherichia coli BL21 using L-Trp as substrate incubated for 30 mins by enzymatic assay	B	4.94	pIC50	11580	nM	IC50	Bioorg Med Chem Lett (2020) 30: 127159-127159 [PMID:32247733]
ChEMBL	Inhibition of N-terminal His-tagged recombinant human TDO extracted from Escherichia coli Transetta (DE3) using L-tryptophan as substrate preincubated for 5 mins followed by substrate addition and measured after 1 hrs by absorbance based microplate reader	B	5.09	pIC50	8070	nM	IC50	Eur J Med Chem (2024) 279: 116852-116852 [PMID:39276584]
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	5.1	pIC50	7943	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 measured after 40 mins by methylene blue reagent based spectrophotometry	B	5.21	pIC50	6100	nM	IC50	J Med Chem (2021) 64: 10967-10980 [PMID:34338527]
ChEMBL	Inhibition of human TDO	B	5.7	pIC50	2000	nM	IC50	Eur J Med Chem (2022) 241: 114625-114625 [PMID:35952399]
ChEMBL	Inhibition of human TDO2 expressed in mouse P815B cells assessed as kynurenine concentration formation using L-tryptophan as substrate incubated for 7 hrs by UPLC analysis	B	5.76	pIC50	1740	nM	IC50	J Med Chem (2021) 64: 10967-10980 [PMID:34338527]
ChEMBL	Inhibition of human TDO transfected in HEK293T cells using L-tryptophan as substrate incubated for 24 hrs by absorbance based microplate analysis	B	5.91	pIC50	1240	nM	IC50	Eur J Med Chem (2024) 279: 116852-116852 [PMID:39276584]
ChEMBL	Inhibition of TDO in human U87 MG cells using L-Trp as substrate after 8 hrs	B	6.17	pIC50	671	nM	IC50	Eur J Med Chem (2018) 160: 133-145 [PMID:30321802]
ChEMBL	Inhibition of human TDO	B	6.21	pIC50	620	nM	IC50	J Med Chem (2015) 58: 8762-8782 [PMID:26207924]
ChEMBL	Inhibition of human recombinant pEF6/V5-His-tagged TDO2 transfected in HEK293-EBNA cells using L-tryptophan as substrate by HPLC analysis	B	6.21	pIC50	620	nM	IC50	J Med Chem (2019) 62: 9161-9174 [PMID:31580660]
GtoPdb	Concentration inhibiting TDO activity by 50% in a cellular assay, at 80μM L-tryptophan.	-	6.21	pIC50	620	nM	IC50	Proc Natl Acad Sci USA (2012) 109: 2497-502 [PMID:22308364]
ChEMBL	Inhibition of TDO (unknown origin) expressed in HEK293 cells using L-Trp as substrate after 8 hrs	B	6.4	pIC50	398	nM	IC50	Eur J Med Chem (2018) 160: 133-145 [PMID:30321802]
ChEMBL	Inhibition of full length N-terminal/C-terminal his-tagged human TDO expressed in Escherichia coli BL21 (DE3) assessed as N-formylkynurenine formation using L-tryptophan as substrate by UV2100 spectrophotometer analysis	B	6.52	pIC50	300	nM	IC50	J Med Chem (2024) 67: 14543-14552 [PMID:39106326]
tryptophan 2,3-dioxygenase/Tryptophan 2,3-dioxygenase in Mouse (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1075307] [GtoPdb: 2887] [UniProtKB: P48776]
ChEMBL	Inhibition of mouse TDO in P815 clone 12 cells by HPLC analysis	B	4.77	pIC50	17000	nM	IC50	J Med Chem (2012) 55: 5270-5290 [PMID:22616902]
ChEMBL	Inhibition of mouse TDO expressed in mouse P815B cells assessed as inhibition of tryptophan catabolism by measuring kynurenine production after 8 hrs by HPLC analysis	B	5.7	pIC50	2000	nM	IC50	J Med Chem (2011) 54: 5320-5334 [PMID:21726069]
ChEMBL	Inhibition of mouse TDO	B	5.71	pIC50	1960	nM	IC50	J Med Chem (2015) 58: 8762-8782 [PMID:26207924]
GtoPdb	Concentration inhibiting TDO activity by 50% in a cellular assay, at 80μM L-tryptophan.	-	5.71	pIC50	1960	nM	IC50	Proc Natl Acad Sci USA (2012) 109: 2497-502 [PMID:22308364]

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]