Research workbench
AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit alpha (P51167)
Analyse AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P51167
- Type
- protein
- Length
- 632 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Amiloride-sensitive sodium channel subunit alpha
- UniProt
- P51167
- Pockets
- 8 · best druggability 0.71
Structure
1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit alpha | protein | 632 | 33% helix, 19% strand | P51167 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 663 | 0.71 | 0.78 | 65 | empty |
| 2 | 336 | 0.63 | 0.79 | 33 | empty |
| 3 | 225 | 0.53 | 0.77 | 22 | empty |
| 4 | 235 | 0.49 | 0.74 | 29 | empty |
| 5 | 58 | 0.46 | 0.84 | 16 | empty |
Modifications
Observed in the structure: 8 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 P51167
- Elsewhere: UniProt P51167 · AlphaFold DB P51167
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