Research workbench
AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit beta (P51169)
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
- P51169
- Type
- protein
- Length
- 647 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Amiloride-sensitive sodium channel subunit beta
- UniProt
- P51169
- Pockets
- 8 · best druggability 0.72
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit beta | protein | 647 | 39% helix, 20% strand | P51169 |
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 | 485 | 0.72 | 0.81 | 54 | empty |
| 2 | 217 | 0.59 | 0.80 | 25 | empty |
| 3 | 289 | 0.55 | 0.76 | 29 | empty |
| 4 | 180 | 0.49 | 0.77 | 32 | empty |
| 5 | 146 | 0.46 | 0.75 | 22 | 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 P51169
- Elsewhere: UniProt P51169 · AlphaFold DB P51169
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