Research workbench
AlphaFold monomer V2.0 prediction for ral GTPase-activating protein subunit beta (Q86X10)
Analyse AlphaFold monomer V2.0 prediction for ral GTPase-activating protein subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q86X10
- Type
- protein
- Length
- 1,494 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x442Bc55C6D07c5f11D2798821a504d57d5208A2c
- Molecule
- Ral GTPase-activating protein subunit beta
- UniProt
- Q86X10
- Pockets
- 18 · best druggability 0.80
Structure
1 distinct chain · 46% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ral GTPase-activating protein subunit beta | protein | 1494 | 46% helix, 5% strand | Q86X10 |
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1170 | 0.80 | 0.81 | 93 | empty |
| 2 | 514 | 0.79 | 0.86 | 61 | empty |
| 3 | 833 | 0.77 | 0.80 | 101 | empty |
| 4 | 67 | 0.69 | 0.96 | 20 | empty |
| 5 | 475 | 0.65 | 0.78 | 45 | 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 Q86X10
- Elsewhere: UniProt Q86X10 · AlphaFold DB Q86X10
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