Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 209 (Q96SK2)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 209 (Q96SK2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96SK2
- Type
- protein
- Length
- 561 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Transmembrane protein 209
- UniProt
- Q96SK2
- Pockets
- 5 · best druggability 0.61
Structure
1 distinct chain · 43% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 209 | protein | 561 | 43% helix, 4% strand | Q96SK2 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.61 | 0.75 | 46 | empty |
| 2 | 106 | 0.51 | 0.82 | 19 | empty |
| 3 | 116 | 0.41 | 0.76 | 25 | empty |
| 4 | 66 | 0.38 | 0.79 | 14 | empty |
| 5 | 100 | 0.36 | 0.74 | 25 | 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 Q96SK2
- Elsewhere: UniProt Q96SK2 · AlphaFold DB Q96SK2
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