Research workbench
AlphaFold monomer V2.0 prediction for transient receptor potential cation channel subfamily V member 3 (Q8NET8)
Analyse AlphaFold monomer V2.0 prediction for transient receptor potential cation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8NET8
- Type
- protein
- Length
- 790 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Transient receptor potential cation channel subfamily V member 3
- UniProt
- Q8NET8
- Pockets
- 11 · best druggability 0.67
Structure
1 distinct chain · 53% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transient receptor potential cation channel subfamily V member 3 | protein | 790 | 53% helix, 4% strand | Q8NET8 |
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.67 | 0.84 | 25 | empty |
| 2 | 455 | 0.66 | 0.78 | 45 | empty |
| 3 | 495 | 0.65 | 0.77 | 44 | empty |
| 4 | 551 | 0.63 | 0.75 | 44 | empty |
| 5 | 351 | 0.60 | 0.77 | 40 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 8V6K · Apo-state cryo-EM structure of human TRPV3 in cNW30 nanodiscs · an experimental structure of the same protein · chain A against B, TM-score 0.79
- 8V6M · Inactivated-state cryo-EM structure of human TRPV3 in presence of tetrahydrocannabivarin… · an experimental structure of the same protein · chain A against A, TM-score 0.78
- 8V6L · Open-state cryo-EM structure of human TRPV3 in presence of tetrahydrocannabivarin (THCV)… · an experimental structure of the same protein · chain A against A, TM-score 0.77
- 8GKA · Human TRPV3 tetramer structure, closed conformation · an experimental structure of the same protein · chain A against B, TM-score 0.77
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 Q8NET8
- Elsewhere: UniProt Q8NET8 · AlphaFold DB Q8NET8
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