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AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit alpha (H1AFJ5)
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
- H1AFJ5
- Type
- protein
- Length
- 655 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x16e07C76957A2F24F14ACC5393e231dF9b8720B9
- Molecule
- Amiloride-sensitive sodium channel subunit alpha
- UniProt
- H1AFJ5
- Pockets
- 11 · best druggability 0.62
Structure
1 distinct chain · 32% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit alpha | protein | 655 | 32% helix, 18% strand | H1AFJ5 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 409 | 0.62 | 0.77 | 44 | empty |
| 2 | 244 | 0.56 | 0.77 | 22 | empty |
| 3 | 55 | 0.55 | 0.89 | 16 | empty |
| 4 | 198 | 0.52 | 0.77 | 25 | empty |
| 5 | 95 | 0.39 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 9 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 H1AFJ5
- Elsewhere: UniProt H1AFJ5 · AlphaFold DB H1AFJ5
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