Research workbench
AlphaFold monomer V2.0 prediction for RAS-gef domain-containing family member 1C (Q9D300)
Analyse AlphaFold monomer V2.0 prediction for RAS-gef domain-containing family member… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9D300
- Type
- protein
- Length
- 466 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- RAS-gef domain-containing family member 1C
- UniProt
- Q9D300
- Pockets
- 6 · best druggability 0.65
Structure
1 distinct chain · 63% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-gef domain-containing family member 1C | protein | 466 | 63% helix, 2% strand | Q9D300 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 379 | 0.65 | 0.79 | 41 | empty |
| 2 | 386 | 0.63 | 0.78 | 57 | empty |
| 3 | 108 | 0.54 | 0.83 | 18 | empty |
| 4 | 99 | 0.40 | 0.77 | 17 | empty |
| 5 | 80 | 0.37 | 0.76 | 14 | 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 Q9D300
- Elsewhere: UniProt Q9D300 · AlphaFold DB Q9D300
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