Research workbench
AlphaFold monomer V2.0 prediction for protein SEY1 (A2QR20)
Analyse AlphaFold monomer V2.0 prediction for protein SEY1 (A2QR20) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2QR20
- Type
- protein
- Length
- 858 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Protein SEY1
- UniProt
- A2QR20
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein SEY1 | protein | 858 | 58% helix, 6% strand | A2QR20 |
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 351 | 0.66 | 0.80 | 38 | empty |
| 2 | 95 | 0.60 | 0.87 | 20 | empty |
| 3 | 134 | 0.57 | 0.83 | 21 | empty |
| 4 | 133 | 0.56 | 0.83 | 26 | empty |
| 5 | 86 | 0.52 | 0.84 | 15 | 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 A2QR20
- Elsewhere: UniProt A2QR20 · AlphaFold DB A2QR20
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