Research workbench
AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruva (Q8EWC5)
Analyse AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8EWC5
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Holliday junction ATP-dependent DNA helicase ruva
- UniProt
- Q8EWC5
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holliday junction ATP-dependent DNA helicase ruva | protein | 219 | 47% helix, 19% strand | Q8EWC5 |
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 | 65 | 0.42 | 0.81 | 16 | empty |
| 2 | 99 | 0.40 | 0.77 | 17 | empty |
| 3 | 69 | 0.30 | 0.74 | 15 | 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 Q8EWC5
- Elsewhere: UniProt Q8EWC5 · AlphaFold DB Q8EWC5
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