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
|
Q9Y4B6 |
DCAF1_HUMAN
Homo sapiens
DDB1- and CUL4-associated factor 1
|
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.
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