Research workbench
AlphaFold monomer V2.0 prediction for formamidopyrimidine-DNA glycosylase (A5VTD0)
Analyse AlphaFold monomer V2.0 prediction for formamidopyrimidine-DNA glycosylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VTD0
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d1188D30c5f312851Bc3459adef3C74f39a2A61
- Molecule
- Formamidopyrimidine-DNA glycosylase
- UniProt
- A5VTD0
- Pockets
- 3 · best druggability 0.43
Structure
1 distinct chain · 28% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formamidopyrimidine-DNA glycosylase | protein | 293 | 28% helix, 25% strand | A5VTD0 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.43 | 0.77 | 20 | empty |
| 2 | 151 | 0.42 | 0.75 | 22 | empty |
| 3 | 86 | 0.34 | 0.74 | 18 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A5VTD0
- Elsewhere: UniProt A5VTD0 · AlphaFold DB A5VTD0
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