Research workbench
AlphaFold monomer V2.0 prediction for sodium channel protein type 1 subunit alpha (A2APX8)
Analyse AlphaFold monomer V2.0 prediction for sodium channel protein type 1 subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2APX8
- Type
- protein
- Length
- 2,009 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Sodium channel protein type 1 subunit alpha
- UniProt
- A2APX8
- Pockets
- 20 · best druggability 0.86
Structure
1 distinct chain · 53% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sodium channel protein type 1 subunit alpha | protein | 2009 | 53% helix, 4% strand | A2APX8 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1083 | 0.86 | 0.87 | 93 | empty |
| 2 | 856 | 0.74 | 0.78 | 75 | empty |
| 3 | 667 | 0.74 | 0.80 | 56 | empty |
| 4 | 499 | 0.68 | 0.79 | 46 | empty |
| 5 | 399 | 0.64 | 0.78 | 38 | empty |
Modifications
Observed in the structure: 6 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 A2APX8
- Elsewhere: UniProt A2APX8 · AlphaFold DB A2APX8
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