Research workbench
AlphaFold monomer V2.0 prediction for receptor-like protein 20 (Q9SKK5)
Analyse AlphaFold monomer V2.0 prediction for receptor-like protein 20 (Q9SKK5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9SKK5
- Type
- protein
- Length
- 671 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xED4FB567cf5C5AEfdc2B6dE952885bE78054A984
- Molecule
- Receptor-like protein 20
- UniProt
- Q9SKK5
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 20% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-like protein 20 | protein | 671 | 20% helix, 21% strand | Q9SKK5 |
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 | 1103 | 0.74 | 0.77 | 86 | empty |
| 2 | 295 | 0.56 | 0.76 | 40 | empty |
| 3 | 71 | 0.34 | 0.77 | 19 | empty |
| 4 | 52 | 0.33 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q9SKK5
- Elsewhere: UniProt Q9SKK5 · AlphaFold DB Q9SKK5
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