CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.79 | Nucleoside Triphosphate Pyrophosphohydrolase |
|
3.90.79.10 | Nucleoside Triphosphate Pyrophosphohydrolase |
Domain Context
CATH Clusters
| Superfamily | Nucleoside Triphosphate Pyrophosphohydrolase |
| Functional Family | 7,8-dihydro-8-oxoguanine triphosphatase |
Enzyme Information
| 3.6.1.56 |
2-hydroxy-dATP diphosphatase.
based on mapping to UniProt P36639
2-hydroxy-dATP + H(2)O = 2-hydroxy-dAMP + diphosphate.
-!- The enzyme hydrolyzes oxidized purine nucleoside triphosphates such as 2-hydroxy-dATP, thereby preventing their misincorporation into DNA. -!- It can also recognize 8-oxo-dGTP and 8-oxo-dATP, but with lower efficiency (cf. EC 3.6.1.55).
|
| 3.6.1.55 |
8-oxo-dGTP diphosphatase.
based on mapping to UniProt P36639
8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.
-!- This enzyme hydrolyzes the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. -!- It does not hydrolyze 2-hydroxy-dATP (cf. EC 3.6.1.56).
|
UniProtKB Entries (1)
| P36639 |
8ODP_HUMAN
Homo sapiens
7,8-dihydro-8-oxoguanine triphosphatase
|
PDB Structure
| PDB | 5NGR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Fragment-Based Discovery and Optimization of Enzyme Inhibitors by Docking of Commercial Chemical Space.
J. Med. Chem.
|
