Research workbench
Crystal structure of the TRPV2 ion channel in complex with rtx
Analyse Crystal structure of the TRPV2 ion channel in complex with rtx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BWJ
- Type
- protein
- Length
- 1,227 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
- G1SNM3
- Ligands
- 6EU, CA
- Pockets
- 15 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transient receptor potential cation channel subfamily V member 2 | protein | 610 | 58% helix, 6% strand | G1SNM3 |
| B | Transient receptor potential cation channel subfamily V member 2 | protein | 617 | 58% helix, 6% strand | G1SNM3 |
Ligands and binding sites
- 6EU · resiniferatoxin · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.80 | 0.81 | 95 | empty |
| 2 | 446 | 0.79 | 0.87 | 33 | empty |
| 3 | 640 | 0.70 | 0.78 | 68 | empty |
| 4 | 300 | 0.65 | 0.80 | 35 | 6EU |
| 5 | 228 | 0.64 | 0.83 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 2583 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6BWJ · Crystal structure of the TRPV2 ion channel in complex with RTx · 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 G1SNM3
- Elsewhere: RCSB PDB 6BWJ · PDBe 6BWJ · UniProt G1SNM3
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