Research workbench
AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruvb (Q2FG86)
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
- Q2FG86
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x87aD4E3aa8116A59bb2fD5A498235D57C8a4cAaA
- Molecule
- Holliday junction ATP-dependent DNA helicase ruvb
- UniProt
- Q2FG86
- Pockets
- 4 · best druggability 0.75
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 | Q2FG86 |
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 | 512 | 0.75 | 0.83 | 49 | empty |
| 2 | 50 | 0.35 | 0.79 | 12 | empty |
| 3 | 95 | 0.33 | 0.73 | 19 | empty |
| 4 | 73 | 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 Q2FG86
- Elsewhere: UniProt Q2FG86 · AlphaFold DB Q2FG86
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