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Ligands
Code Name Style Show Link
C82 ~{N}-(4-chlorophenyl)-1~{H}-1,2,3-triazol-5-amine
ALA Alanine
HEM Protoporphyrin ix containing Fe
Non-standard Residues
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Glycosylation
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Code : 6F0A   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Crystal structure of human indoleamine 2,3-dioxygenase bound to a triazole inhibitor and alanine molecule.
Release Data : 2017-12-27
Compound :
mol_id molecule chains synonym
1 Indoleamine 2,3-dioxygenase 1 A,C IDO-1,Indoleamine-pyrrole 2,3-dioxygenase
ec: 1.13.11.52
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: IDO1, IDO, INDO
expression_system_plasmid: pET28
Authors : Swan, M.K., Latchem, M.
Keywords : Tryptophan 2 3 Dioxygenase Activity Electron Transfer Activity Oxidoreductase Activity Heme Binding Indoleamine 2 3 Dioxygenase Activity Metal Ion Binding Dioxygenase Activity, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.2600 Å )
Citation :

New 4-Amino-1,2,3-Triazole Inhibitors of Indoleamine 2,3-Dioxygenase Form a Long-Lived Complex with the Enzyme and Display Exquisite Cellular Potency.

Alexandre, J.A.C.,Swan, M.K.,Latchem, M.J.  et al.
(2018)  Chembiochem  19 : 552 - 561

PubMed: 29240291
DOI: 10.1002/cbic.201700560

Chain : A, C
UniProt : P14902 (I23O1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
D-tryptophan + O2 = N-formyl-D-kynurenine 1.13.11.52 PubMed:17671174
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L-tryptophan + O2 = N-formyl-L-kynurenine 1.13.11.52 PubMed:17671174
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