Research workbench
AlphaFold monomer V2.0 prediction for RAS-related protein rab-3C (Q96E17)
Analyse AlphaFold monomer V2.0 prediction for RAS-related protein rab-3C (Q96E17) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96E17
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- RAS-related protein rab-3C
- UniProt
- Q96E17
- Pockets
- 2 · best druggability 0.57
Structure
1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rab-3C | protein | 227 | 36% helix, 22% strand | Q96E17 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.57 | 0.81 | 30 | empty |
| 2 | 63 | 0.31 | 0.75 | 11 | empty |
Compared structures
- 6Y7G · Structure of the human RAB3C in complex with GDP · an experimental structure of the same protein · chain A against B, TM-score 0.69
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 Q96E17
- Elsewhere: UniProt Q96E17 · AlphaFold DB Q96E17
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.