Research workbench
AlphaFold monomer V2.0 prediction for RAS-gef domain-containing family member 1B (Q28EC1)
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
- Q28EC1
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- RAS-gef domain-containing family member 1B
- UniProt
- Q28EC1
- Pockets
- 8 · best druggability 0.63
Structure
1 distinct chain · 67% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-gef domain-containing family member 1B | protein | 472 | 67% helix, 3% strand | Q28EC1 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.63 | 0.81 | 36 | empty |
| 2 | 144 | 0.46 | 0.77 | 26 | empty |
| 3 | 214 | 0.46 | 0.74 | 20 | empty |
| 4 | 118 | 0.46 | 0.78 | 17 | empty |
| 5 | 179 | 0.45 | 0.74 | 23 | 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 Q28EC1
- Elsewhere: UniProt Q28EC1 · AlphaFold DB Q28EC1
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