MolNFT v1 · #421501 · protein
AlphaFold monomer V2.0 prediction for sodium channel protein type 3 subunit alpha (Q9NY46)
Q9NY46: “AlphaFold monomer V2.0 prediction for sodium channel protein type 3 subunit alpha (Q9NY46)”. 20 pockets (best druggability 0.86). MolNFT v1 #421501 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q9NY46
- Type
- protein
- Length
- 2,000 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6e01080e01Da0b8798c9B0Ea0E75d75D9e49F5Df
- Molecule
- Sodium channel protein type 3 subunit alpha
- UniProt
- Q9NY46
- Pockets
- 20 · best druggability 0.86
Structure
1 distinct chain · 53% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sodium channel protein type 3 subunit alpha | protein | 2000 | 53% helix, 3% strand | Q9NY46 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1107 | 0.86 | 0.86 | 94 | empty |
| 2 | 485 | 0.73 | 0.82 | 50 | empty |
| 3 | 1057 | 0.73 | 0.76 | 71 | empty |
| 4 | 627 | 0.71 | 0.79 | 52 | empty |
| 5 | 534 | 0.70 | 0.79 | 51 | empty |
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 7W77 · Cryo-EM structure of human NAV1.3/BETA1/BETA2-bulleyaconitinea · an experimental structure of the same protein · chain A against D, TM-score 0.56
- 7W77 · cryo-EM structure of human NaV1.3/beta1/beta2-bulleyaconitineA · an experimental structure of the same protein · chain A against D, TM-score 0.56
- 7W7F · Cryo-EM structure of human NAV1.3/BETA1/BETA2-ICA121431 · an experimental structure of the same protein · chain A against D, TM-score 0.55
- 7W7F · Cryo-EM structure of human NaV1.3/beta1/beta2-ICA121431 · an experimental structure of the same protein · chain A against D, TM-score 0.55
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 Q9NY46
- Elsewhere: UniProt Q9NY46 · AlphaFold DB Q9NY46
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