Research workbench
Cryo-EM structure of the C2-symmetric TRPV2/RTX complex in nanodiscs
Analyse Cryo-EM structure of the C2-symmetric TRPV2/RTX complex in nanodiscs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OO7
- Type
- protein
- Length
- 2,394 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G1SNM3
- Ligands
- 6EU
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 602 | — | G1SNM3 |
| B, D | — | protein | 595 | — | G1SNM3 |
Ligands and binding sites
- 6EU · resiniferatoxin · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OO7 · Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in nanodiscs · 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 6OO7 · PDBe 6OO7 · UniProt G1SNM3
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