Research workbench
Crystal structure of the ankyrin repeat domain of human TRPV2
Analyse Crystal structure of the ankyrin repeat domain of human TRPV2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F37
- Type
- protein
- Length
- 496 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 2
- UniProt
- Q9Y5S1
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transient receptor potential cation channel subfamily V member 2 | protein | 247 | 52% helix, 2% strand | Q9Y5S1 |
| B | Transient receptor potential cation channel subfamily V member 2 | protein | 249 | 52% helix, 2% strand | Q9Y5S1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.68 | 0.80 | 51 | empty |
| 2 | 201 | 0.57 | 0.80 | 36 | empty |
| 3 | 130 | 0.55 | 0.82 | 28 | empty |
| 4 | 75 | 0.35 | 0.76 | 18 | empty |
| 5 | 52 | 0.25 | 0.73 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 983 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2F37 · Crystal structure of the ankyrin repeat domain of human TRPV2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y5S1 · 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 Q9Y5S1
- Elsewhere: RCSB PDB 2F37 · PDBe 2F37 · UniProt Q9Y5S1
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