CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.20 | Up-down Bundle | |
1.20.58 | Methane Monooxygenase Hydroxylase; Chain G, domain 1 | |
1.20.58.480 |
Domain Context
CATH Clusters
Superfamily | 1.20.58.480 |
Functional Family |
Enzyme Information
1.13.11.52 |
Indoleamine 2,3-dioxygenase.
based on mapping to UniProt P14902
(1) D-tryptophan + O(2) = N-formyl-D-kynurenine. (2) L-tryptophan + O(2) = N-formyl-L-kynurenine.
-!- Requires ascorbic acid and methylene blue for activity. -!- Has broader substrate specificity than EC 1.13.11.11. -!- Is induced in response to pathological conditions and host-defense mechanisms. -!- While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan. -!- Superoxide radicals can replace O(2) as oxygen donor.
|
UniProtKB Entries (1)
P14902 |
I23O1_HUMAN
Homo sapiens
Indoleamine 2,3-dioxygenase 1
|
PDB Structure
PDB | 5ETW |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Important Hydrogen Bond Networks in Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitor Design Revealed by Crystal Structures of Imidazoleisoindole Derivatives with IDO1.
J.Med.Chem.
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