Research workbench
AlphaFold monomer V2.0 prediction for sodium channel protein type 10 subunit alpha (P0DMA5)
Analyse AlphaFold monomer V2.0 prediction for sodium channel protein type 10 subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DMA5
- Type
- protein
- Length
- 1,959 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Sodium channel protein type 10 subunit alpha
- UniProt
- P0DMA5
- Pockets
- 20 · best druggability 0.85
Structure
1 distinct chain · 54% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sodium channel protein type 10 subunit alpha | protein | 1959 | 54% helix, 3% strand | P0DMA5 |
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 | 1138 | 0.85 | 0.85 | 83 | empty |
| 2 | 739 | 0.76 | 0.80 | 75 | empty |
| 3 | 734 | 0.73 | 0.79 | 61 | empty |
| 4 | 555 | 0.71 | 0.80 | 44 | empty |
| 5 | 656 | 0.71 | 0.78 | 58 | 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 P0DMA5
- Elsewhere: UniProt P0DMA5 · AlphaFold DB P0DMA5
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