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AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruvb (A1T884)
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
- A1T884
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Holliday junction ATP-dependent DNA helicase ruvb
- UniProt
- A1T884
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holliday junction ATP-dependent DNA helicase ruvb | protein | 355 | 47% helix, 14% strand | A1T884 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.71 | 0.85 | 35 | empty |
| 2 | 101 | 0.49 | 0.82 | 22 | empty |
| 3 | 54 | 0.28 | 0.75 | 11 | 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 A1T884
- Elsewhere: UniProt A1T884 · AlphaFold DB A1T884
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