Research workbench
Structure of human TRPV3 in the presence of 2-apb in C2 symmetry (2)
Analyse Structure of human TRPV3 in the presence of 2-apb in C2 symmetry (2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MHX
- Type
- protein
- Length
- 2,436 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 0.79
Structure
electron microscopy · 1 distinct chain · 60% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | Transient receptor potential cation channel subfamily V member 3 | protein | 609 | 60% helix, 5% 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 | 437 | 0.79 | 0.86 | 60 | empty |
| 2 | 788 | 0.79 | 0.82 | 84 | empty |
| 3 | 922 | 0.78 | 0.80 | 88 | empty |
| 4 | 528 | 0.77 | 0.84 | 65 | empty |
| 5 | 881 | 0.77 | 0.79 | 78 | empty |
Interfaces
4 interfaces between chains.
- C–D · 2490 Ų buried · 10 hydrogen bonds · protein-protein
- B–A · 2483 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 2289 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 2287 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6MHX · Structure of human TRPV3 in the presence of 2-APB in C2 symmetry (2) · the same entry in another collection · chain B against B, TM-score 1.00
- Q8NET8 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 6MHX · PDBe 6MHX · UniProt Q8NET8
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