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AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit beta (H1AFJ6)
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
- H1AFJ6
- Type
- protein
- Length
- 651 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d10233e8d7916EAcA13bcc0a521cCa504C4dDE7
- Molecule
- Amiloride-sensitive sodium channel subunit beta
- UniProt
- H1AFJ6
- Pockets
- 7 · best druggability 0.70
Structure
1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit beta | protein | 651 | 39% helix, 19% strand | H1AFJ6 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 474 | 0.70 | 0.80 | 58 | empty |
| 2 | 273 | 0.59 | 0.78 | 35 | empty |
| 3 | 126 | 0.48 | 0.79 | 22 | empty |
| 4 | 154 | 0.47 | 0.77 | 24 | empty |
| 5 | 108 | 0.36 | 0.74 | 18 | 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 H1AFJ6
- Elsewhere: UniProt H1AFJ6 · AlphaFold DB H1AFJ6
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