CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.150 | Divalent-metal-dependent TIM barrel enzymes |
Domain Context
CATH Clusters
| Superfamily | Divalent-metal-dependent TIM barrel enzymes |
| Functional Family | Probable endonuclease 4 |
Enzyme Information
| 3.1.21.2 |
Deoxyribonuclease IV.
based on mapping to UniProt P0A6C1
Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
-!- The enzyme is an apurinic/apyrimidinic (AP) site endonuclease that primes DNA repair synthesis at AP sites. -!- It specifically cleaves the DNA backbone at AP sites and also removes 3' DNA-blocking groups such as 3' phosphates, 3' phosphoglycolates, and 3' alpha,beta-unsaturated aldehydes that arise from oxidative base damage and the activity of combined glycosylase/lyase enzymes. -!- It is also the only known repair enzyme that is able to cleave the DNA backbone 5' of the oxidative lesion alpha-deoxyadenosine. -!- The enzyme has a strong preference for single-stranded DNA. -!- Formerly EC 3.1.4.30.
|
UniProtKB Entries (1)
| P0A6C1 |
END4_ECOLI
Escherichia coli K-12
Endonuclease 4
|
PDB Structure
| PDB | 1QTW |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis.
Cell(Cambridge,Mass.)
|
