MolNFT v1 · #83158 · protein
Crystal structure of the ankyrin repeat domain of chicken TRPV4
3W9G · Vanilloid receptor-related osmotically activated channel…: “Crystal structure of the ankyrin repeat domain of chicken TRPV4”. X-ray diffraction, 7 pockets (best druggability 0.56). MolNFT v1 #83158 on GenesisL1: 3D structure…
- PDB
- 3W9G
- Type
- protein
- Length
- 1,016 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vanilloid receptor-related osmotically activated channel protein
- UniProt
- Q9DFS3
- Pockets
- 7 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 53% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Vanilloid receptor-related osmotically activated channel protein | protein | 256 | 53% helix, 4% strand | Q9DFS3 |
| C | Vanilloid receptor-related osmotically activated channel protein | protein | 252 | 54% helix, 3% strand | Q9DFS3 |
| D | Vanilloid receptor-related osmotically activated channel protein | protein | 252 | 53% helix, 3% strand | Q9DFS3 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.56 | 0.77 | 27 | empty |
| 2 | 165 | 0.48 | 0.77 | 23 | empty |
| 3 | 154 | 0.47 | 0.77 | 22 | empty |
| 4 | 119 | 0.46 | 0.78 | 17 | empty |
| 5 | 95 | 0.41 | 0.77 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 482 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 406 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 169 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3W9G · Crystal structure of the ankyrin repeat domain of chicken TRPV4 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9DFS3
- Elsewhere: RCSB PDB 3W9G · PDBe 3W9G · UniProt Q9DFS3
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