MolNFT v1 · #122684 · protein
Structure of transient receptor potential (TRP) channel TRPV6 in the presence of calcium
5IWP · Transient receptor potential cation channel subfamily V…: “Structure of transient receptor potential (TRP) channel TRPV6 in the presence of calcium”. X-ray diffraction, 2 ligands (DTB, CA), 9 pockets (best druggability 0.74). MolNFT…
- PDB
- 5IWP
- Type
- protein
- Length
- 591 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 6
- UniProt
- Q9R186
- Ligands
- DTB, CA
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transient receptor potential cation channel subfamily V member 6 | protein | 591 | 55% helix, 5% strand | Q9R186 |
Ligands and binding sites
- DTB · 6-(5-methyl-2-oxo-imidazolidin-4-yl)-hexanoic acid · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 656 | 0.74 | 0.80 | 60 | empty |
| 2 | 268 | 0.68 | 0.83 | 30 | empty |
| 3 | 402 | 0.65 | 0.78 | 43 | empty |
| 4 | 197 | 0.54 | 0.78 | 25 | DTB |
| 5 | 133 | 0.48 | 0.78 | 22 | empty |
Compared structures
- 5IWP · Structure of Transient Receptor Potential (TRP) channel TRPV6 in the presence of calcium · the same entry in another collection · chain A against A, TM-score 1.00
- Q9R186 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q9R186
- Elsewhere: RCSB PDB 5IWP · PDBe 5IWP · UniProt Q9R186
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