MolNFT v1 · #156877 · protein
Structure of human TRPV3 in the presence of 2-apb in C2 symmetry (1)
6MHW · Transient receptor potential cation channel subfamily V…: “Structure of human TRPV3 in the presence of 2-apb in C2 symmetry (1)”. Electron microscopy, 20 pockets (best druggability 0.77). MolNFT v1 #156877 on GenesisL1: 3D…
- PDB
- 6MHW
- Type
- protein
- Length
- 2,452 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 0.77
Structure
electron microscopy · 1 distinct chain · 60% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 3 | protein | 613 | 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 | 365 | 0.77 | 0.86 | 47 | empty |
| 2 | 1011 | 0.76 | 0.78 | 71 | empty |
| 3 | 959 | 0.75 | 0.78 | 72 | empty |
| 4 | 454 | 0.72 | 0.82 | 33 | empty |
| 5 | 226 | 0.72 | 0.87 | 29 | empty |
Interfaces
4 interfaces between chains.
- A–D · 2597 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 2594 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 2410 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 2392 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6MHW · Structure of human TRPV3 in the presence of 2-APB in C2 symmetry (1) · 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 0.98
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 6MHW · PDBe 6MHW · UniProt Q8NET8
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