Research workbench
Cryo-EM structure of mouse TRPV3
Analyse Cryo-EM structure of mouse TRPV3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DVW
- Type
- protein
- Length
- 2,576 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
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 53% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 3 | protein | 644 | 53% helix, 2% strand | Q8K424 |
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 | 970 | 0.85 | 0.85 | 101 | empty |
| 2 | 816 | 0.79 | 0.82 | 78 | empty |
| 3 | 1010 | 0.78 | 0.80 | 83 | empty |
| 4 | 1057 | 0.78 | 0.80 | 90 | empty |
| 5 | 837 | 0.77 | 0.80 | 70 | empty |
Interfaces
4 interfaces between chains.
- A–D · 2850 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 2841 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 2840 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 2834 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 6DVW · PDBe 6DVW · UniProt Q8K424
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