CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.470 | Uracil-DNA Glycosylase, subunit E |
|
3.40.470.10 | Uracil-DNA glycosylase-like domain |
Domain Context
CATH Clusters
| Superfamily | Uracil-DNA glycosylase-like domain |
| Functional Family | Uracil-DNA glycosylase |
Enzyme Information
| 3.2.2.27 |
Uracil-DNA glycosylase.
based on mapping to UniProt P13051
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
-!- Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. -!- Uracil-DNA glycosylase (EC 3.2.2.27) and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolyzing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalyzing the removal of mis-incorporated uracil from DNA.
|
UniProtKB Entries (2)
| P12520 |
VPR_HV1N5
Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)
Protein Vpr
|
| P13051 |
UNG_HUMAN
Homo sapiens
Uracil-DNA glycosylase
|
PDB Structure
| PDB | 5JK7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction.
Nat.Struct.Mol.Biol.
|
