Research workbench
Cryo-EM structure of the human TRPV3 K169A mutant in the presence of 2-apb, determined in lipid nanodisc
Analyse Cryo-EM structure of the human TRPV3 K169A mutant in the presence of 2-apb… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UW9
- Type
- protein
- Length
- 2,328 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
- Q8NET8
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 58% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 3 | protein | 582 | 58% helix, 3% strand | Q8NET8 |
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 | 906 | 0.83 | 0.84 | 89 | empty |
| 2 | 530 | 0.75 | 0.82 | 51 | empty |
| 3 | 547 | 0.75 | 0.82 | 57 | empty |
| 4 | 513 | 0.75 | 0.82 | 52 | empty |
| 5 | 488 | 0.74 | 0.82 | 44 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2622 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 2617 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 2611 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 2610 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 17 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6UW9 · Cryo-EM structure of the human TRPV3 K169A mutant in the presence of 2-APB, determined in… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NET8 · 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 Q8NET8
- Elsewhere: RCSB PDB 6UW9 · PDBe 6UW9 · UniProt Q8NET8
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