Research workbench
AlphaFold monomer V2.0 prediction for rho-related GTP-binding protein rhou (Q9EQT3)
Analyse AlphaFold monomer V2.0 prediction for rho-related GTP-binding protein rhou… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9EQT3
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd4b26826943B18d73BEAc264FD887536a26907B8
- Molecule
- Rho-related GTP-binding protein rhou
- UniProt
- Q9EQT3
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 30% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-related GTP-binding protein rhou | protein | 261 | 30% helix, 17% strand | Q9EQT3 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.69 | 0.90 | 35 | empty |
| 2 | 209 | 0.56 | 0.79 | 32 | empty |
| 3 | 98 | 0.37 | 0.76 | 16 | empty |
| 4 | 68 | 0.28 | 0.73 | 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 Q9EQT3
- Elsewhere: UniProt Q9EQT3 · AlphaFold DB Q9EQT3
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