Research workbench
AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruva (A6LFB5)
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
- A6LFB5
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x57A3AcB7C91DdfC3398a5ED45008eC8bd397c6c0
- Molecule
- Holliday junction ATP-dependent DNA helicase ruva
- UniProt
- A6LFB5
- Pockets
- 2 · best druggability 0.44
Structure
1 distinct chain · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holliday junction ATP-dependent DNA helicase ruva | protein | 196 | 48% helix, 20% strand | A6LFB5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.44 | 0.79 | 17 | empty |
| 2 | 73 | 0.35 | 0.77 | 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 A6LFB5
- Elsewhere: UniProt A6LFB5 · AlphaFold DB A6LFB5
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