› 5yx9

Electron Microscopy
3.8Å resolution

Cryo-EM structure of human TRPC6 at 3.8A resolution

Released:
DOI: 10.2210/pdb5yx9/pdb
PDB entry 5yx9 coloured by chain, front view.
PDB entry 5yx9 coloured by chain, side view.
PDB entry 5yx9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the receptor-activated human TRPC6 and TRPC3 ion channels.
Tang Q, Guo W, Zheng L, Wu JX, Liu M, Zhou X, Zhang X, Chen L
Cell Res 28 746-755 (2018)
PMID: 29700422
Related structures: EMD-6856

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short transient receptor potential channel 6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 931 amino acids
Theoretical weight: 106.45 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9Y210 (Residues: 1-931; Coverage: 100%)
Gene names: TRP6, TRPC6
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-6856
Expression system: Homo sapiens

Quick links

Citations

35 review citations

TRPC channels: Structure, function, regulation and recent advances in small molecular probes.
Wang et al. (2020)
34 more

14 mentions without citation

Transient Receptor Potential Canonical (TRPC) Channels: Then and Now.
Chen et al. (2020)
13 more