Research workbench
Crystal structure of rat TRPV6*- in complex with brominated 2- aminoethoxydiphenyl borate (2-apb-br)
Analyse Crystal structure of rat TRPV6*- in complex with brominated 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D7V
- Type
- protein
- Length
- 592 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
- FYY, CA
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transient receptor potential cation channel subfamily V member 6 | protein | 592 | 54% helix, 3% strand | Q9R186 |
Ligands and binding sites
- FYY · 2-aminoethyl (4-bromophenyl)phenylborinate · 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
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 548 | 0.66 | 0.77 | 48 | FYY |
| 2 | 193 | 0.65 | 0.85 | 27 | empty |
| 3 | 201 | 0.55 | 0.79 | 28 | empty |
| 4 | 95 | 0.46 | 0.80 | 17 | empty |
| 5 | 75 | 0.46 | 0.82 | 12 | empty |
Compared structures
- 6D7V · Crystal Structure of Rat TRPV6*- in complex with brominated 2-Aminoethoxydiphenyl borate… · 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 0.97
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 6D7V · PDBe 6D7V · UniProt Q9R186
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