› 6cud

Electron Microscopy
3.3Å resolution

Structure of the human TRPC3 in a lipid-occupied, closed state

Released:
DOI: 10.2210/pdb6cud/pdb
PDB entry 6cud coloured by chain, front view.
PDB entry 6cud coloured by chain, side view.
PDB entry 6cud coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the human lipid-gated cation channel TRPC3.
Fan C, Choi W, Sun W, Du J, Lu W
Elife 7 (2018)
PMID: 29726814
Related structures: EMD-7620

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-171729 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short transient receptor potential channel 3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 806 amino acids
Theoretical weight: 92.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q13507 (Residues: 86-891; Coverage: 88%)
Gene names: TRP3, TRPC3
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand 6OE 4 x 6OE
Ligand FGJ 4 x FGJ
Ligand NAG 4 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-7620
Expression system: Homo sapiens

Quick links

Citations

22 review citations

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

17 mentions without citation

Advances in TRP channel drug discovery: from target validation to clinical studies.
Koivisto et al. (2022)
16 more