Research workbench
AlphaFold monomer V2.0 prediction for sodium channel protein type 4 subunit alpha a (Q2XVR5)
Analyse AlphaFold monomer V2.0 prediction for sodium channel protein type 4 subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2XVR5
- Type
- protein
- Length
- 1,863 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x75a0B34D1dbc9C40E491eea9b045D34E5f310b57
- Molecule
- Sodium channel protein type 4 subunit alpha a
- UniProt
- Q2XVR5
- Pockets
- 20 · best druggability 0.86
Structure
1 distinct chain · 57% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sodium channel protein type 4 subunit alpha a | protein | 1863 | 57% helix, 3% strand | Q2XVR5 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1180 | 0.86 | 0.87 | 106 | empty |
| 2 | 629 | 0.73 | 0.80 | 59 | empty |
| 3 | 539 | 0.69 | 0.79 | 47 | empty |
| 4 | 477 | 0.68 | 0.79 | 52 | empty |
| 5 | 403 | 0.62 | 0.77 | 36 | empty |
Modifications
Observed in the structure: 6 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 Q2XVR5
- Elsewhere: UniProt Q2XVR5 · AlphaFold DB Q2XVR5
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