Research workbench
AlphaFold monomer V2.0 prediction for topoisomerase 1-associated factor 1 (Q2PIU8)
Analyse AlphaFold monomer V2.0 prediction for topoisomerase 1-associated factor 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2PIU8
- Type
- protein
- Length
- 1,166 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Topoisomerase 1-associated factor 1
- UniProt
- Q2PIU8
- Pockets
- 17 · best druggability 0.83
Structure
1 distinct chain · 56% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Topoisomerase 1-associated factor 1 | protein | 1166 | 56% helix, 3% strand | Q2PIU8 |
Pockets
17 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1192 | 0.83 | 0.84 | 90 | empty |
| 2 | 1148 | 0.75 | 0.78 | 77 | empty |
| 3 | 64 | 0.59 | 0.90 | 18 | empty |
| 4 | 279 | 0.58 | 0.78 | 27 | empty |
| 5 | 72 | 0.50 | 0.84 | 16 | 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 Q2PIU8
- Elsewhere: UniProt Q2PIU8 · AlphaFold DB Q2PIU8
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