Research workbench
AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruva (A8MHI4)
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
- A8MHI4
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDc7b11bC19E7871dc4cc7f885eEd3e0D4eBdc448
- Molecule
- Holliday junction ATP-dependent DNA helicase ruva
- UniProt
- A8MHI4
- Pockets
- 1 · best druggability 0.31
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 | 194 | 48% helix, 20% strand | A8MHI4 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.31 | 0.75 | 12 | 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 A8MHI4
- Elsewhere: UniProt A8MHI4 · AlphaFold DB A8MHI4
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