Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase II subunit 1 (Q7SA95)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase II subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7SA95
- Type
- protein
- Length
- 645 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE506F93E4458Acac5054741df112b789e99Fb9c6
- Molecule
- ATP-dependent DNA helicase II subunit 1
- UniProt
- Q7SA95
- Pockets
- 8 · best druggability 0.77
Structure
1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase II subunit 1 | protein | 645 | 35% helix, 19% strand | Q7SA95 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 844 | 0.77 | 0.81 | 79 | empty |
| 2 | 271 | 0.70 | 0.85 | 25 | empty |
| 3 | 131 | 0.57 | 0.84 | 20 | empty |
| 4 | 239 | 0.53 | 0.76 | 30 | empty |
| 5 | 132 | 0.40 | 0.74 | 21 | 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 Q7SA95
- Elsewhere: UniProt Q7SA95 · AlphaFold DB Q7SA95
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