Research workbench
Cryo-EM structure of mouse TRPV3-Y564A in open state at 37 degrees celsius
Analyse Cryo-EM structure of mouse TRPV3-Y564A in open state at 37 degrees celsius in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PVP
- Type
- protein
- Length
- 2,644 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 3
- UniProt
- Q8K424
- Ligands
- NA
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 1 distinct chain · 53% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 3 | protein | 661 | 53% helix, 1% strand | Q8K424 |
Ligands and binding sites
- NA · Sodium ion · metal
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.81 | 0.82 | 78 | NA |
| 2 | 987 | 0.77 | 0.79 | 109 | empty |
| 3 | 928 | 0.76 | 0.79 | 98 | empty |
| 4 | 995 | 0.76 | 0.79 | 102 | empty |
| 5 | 321 | 0.74 | 0.86 | 46 | empty |
Interfaces
4 interfaces between chains.
- C–D · 3157 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 3062 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 3037 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 2942 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6PVP · Cryo-EM structure of mouse TRPV3-Y564A in open state at 37 degrees Celsius · the same entry in another collection · chain A against A, TM-score 1.00
- Q8K424 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q8K424
- Elsewhere: RCSB PDB 6PVP · PDBe 6PVP · UniProt Q8K424
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