Research workbench
AlphaFold monomer V2.0 prediction for topoisomerase I damage affected protein 4 (P47153)
Analyse AlphaFold monomer V2.0 prediction for topoisomerase I damage affected protein 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P47153
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Topoisomerase I damage affected protein 4
- UniProt
- P47153
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Topoisomerase I damage affected protein 4 | protein | 279 | 74% helix, 0% strand | P47153 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.80 | 0.96 | 27 | empty |
| 2 | 481 | 0.73 | 0.82 | 38 | empty |
| 3 | 50 | 0.35 | 0.79 | 17 | empty |
| 4 | 60 | 0.30 | 0.74 | 14 | 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 P47153
- Elsewhere: UniProt P47153 · AlphaFold DB P47153
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