Research workbench
AlphaFold monomer V2.0 prediction for RAS-related protein rabv (Q54RY4)
Analyse AlphaFold monomer V2.0 prediction for RAS-related protein rabv (Q54RY4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54RY4
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3c860Cd4B4aF5cd0B224EEce054f91b534Db0285
- Molecule
- RAS-related protein rabv
- UniProt
- Q54RY4
- Pockets
- 5 · best druggability 0.60
Structure
1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rabv | protein | 233 | 35% helix, 21% strand | Q54RY4 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.60 | 0.84 | 15 | empty |
| 2 | 253 | 0.59 | 0.79 | 32 | empty |
| 3 | 187 | 0.58 | 0.81 | 31 | empty |
| 4 | 114 | 0.50 | 0.80 | 18 | empty |
| 5 | 57 | 0.29 | 0.74 | 9 | 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 Q54RY4
- Elsewhere: UniProt Q54RY4 · AlphaFold DB Q54RY4
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