Research workbench
AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit alpha (Q92075)
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
- Q92075
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Amiloride-sensitive sodium channel subunit alpha
- UniProt
- Q92075
- Pockets
- 8 · best druggability 0.69
Structure
1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit alpha | protein | 637 | 33% helix, 18% strand | Q92075 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 669 | 0.69 | 0.76 | 61 | empty |
| 2 | 212 | 0.56 | 0.79 | 21 | empty |
| 3 | 216 | 0.47 | 0.74 | 24 | empty |
| 4 | 166 | 0.46 | 0.75 | 27 | empty |
| 5 | 86 | 0.38 | 0.75 | 14 | 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 Q92075
- Elsewhere: UniProt Q92075 · AlphaFold DB Q92075
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