Research workbench
AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruvb (A3D481)
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
- A3D481
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Holliday junction ATP-dependent DNA helicase ruvb
- UniProt
- A3D481
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holliday junction ATP-dependent DNA helicase ruvb | protein | 334 | 51% helix, 14% strand | A3D481 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.70 | 0.86 | 38 | empty |
| 2 | 122 | 0.36 | 0.73 | 19 | empty |
| 3 | 87 | 0.32 | 0.73 | 18 | empty |
| 4 | 54 | 0.31 | 0.77 | 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 A3D481
- Elsewhere: UniProt A3D481 · AlphaFold DB A3D481
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.