CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.360 | Flavodoxin domain |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.360 |
| Functional Family |
Enzyme Information
| 1.10.5.1 |
Ribosyldihydronicotinamide dehydrogenase (quinone).
based on mapping to UniProt P16083
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D- ribofuranosyl)nicotinamide + a quinol.
-!- Unlike EC 1.6.5.2, this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. -!- Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17-beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor. -!- This enzyme can catalyze both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced. -!- Formerly EC 1.10.99.2.
|
UniProtKB Entries (1)
| P16083 |
NQO2_HUMAN
Homo sapiens
Ribosyldihydronicotinamide dehydrogenase [quinone]
|
PDB Structure
| PDB | 4FGJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures of quinone reductase 2 bound to antimalarial drugs reveal conformational change upon reduction
J.Biol.Chem.
|