Research workbench
AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit alpha (P37088)
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
- P37088
- Type
- protein
- Length
- 669 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x934f84D099E5FEaBA89bC58DBEB7366EFF6BF871
- Molecule
- Amiloride-sensitive sodium channel subunit alpha
- UniProt
- P37088
- Pockets
- 11 · best druggability 0.69
Structure
1 distinct chain · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit alpha | protein | 669 | 29% helix, 18% strand | P37088 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.69 | 0.78 | 54 | empty |
| 2 | 122 | 0.56 | 0.83 | 22 | empty |
| 3 | 270 | 0.56 | 0.77 | 28 | empty |
| 4 | 147 | 0.41 | 0.74 | 18 | empty |
| 5 | 51 | 0.40 | 0.82 | 13 | empty |
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6WTH · Full-length human ENAC ecd · an experimental structure of the same protein · chain A against A, TM-score 0.56
- 6WTH · Full-length human ENaC ECD · an experimental structure of the same protein · chain A against A, TM-score 0.56
- 2M3O · Structure and dynamics of a human Nedd4 WW domain-ENaC complex · an experimental structure of the same protein · chain A against P, TM-score 0.01
- 2M3O · Structure and dynamics of a human NEDD4 ww domain-ENAC complex · an experimental structure of the same protein · chain A against P, TM-score 0.01
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 P37088
- Elsewhere: UniProt P37088 · AlphaFold DB P37088
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