Research workbench
Electron cryo-microscopy structure of the canonical TRPC4 ion channel
Analyse Electron cryo-microscopy structure of the canonical TRPC4 ion channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G1K
- Type
- protein
- Length
- 2,592 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- U3N7D8
- Ligands
- Y01, 44E
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 648 | — | U3N7D8 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 4 copies · chains A, B, D, C
- 44E · (2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoate · ligand · 4 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G1K · Electron cryo-microscopy structure of the canonical TRPC4 ion channel · 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 U3N7D8
- Elsewhere: RCSB PDB 6G1K · PDBe 6G1K · UniProt U3N7D8
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