CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1670 | Endonuclease Iii, domain 2 |
|
1.10.1670.10 | Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal) |
Domain Context
CATH Clusters
| Superfamily | Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal) |
| Functional Family | N-glycosylase/DNA lyase OGG1 |
Enzyme Information
| 3.2.2.- |
Hydrolyzing N-glycosyl compounds.
based on mapping to UniProt O15527
|
| 4.2.99.18 |
DNA-(apurinic or apyrimidinic site) lyase.
based on mapping to UniProt O15527
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
-!- 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. -!- This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2.
|
UniProtKB Entries (1)
| O15527 |
OGG1_HUMAN
Homo sapiens
N-glycosylase/DNA lyase
|
PDB Structure
| PDB | 2NOF |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations.
J.Biol.Chem.
|