Research workbench
Crystal structure of transient receptor potential (TRP) channel TRPV6*-DEL1
Analyse Crystal structure of transient receptor potential (TRP) channel TRPV6*-DEL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WO8
- Type
- protein
- Length
- 587 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
- 12 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transient receptor potential cation channel subfamily V member 6 | protein | 587 | 55% helix, 4% strand | Q9R186 |
Ligands and binding sites
- DTB · 6-(5-methyl-2-oxo-imidazolidin-4-yl)-hexanoic acid · ligand · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 485 | 0.72 | 0.81 | 38 | empty |
| 2 | 186 | 0.62 | 0.83 | 26 | empty |
| 3 | 318 | 0.59 | 0.77 | 33 | empty |
| 4 | 221 | 0.57 | 0.79 | 27 | DTB |
| 5 | 143 | 0.50 | 0.79 | 19 | empty |
Compared structures
- 5WO8 · Crystal Structure of Transient Receptor Potential (TRP) channel TRPV6*-Del1 · 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 5WO8 · PDBe 5WO8 · UniProt Q9R186
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