8wpl

Electron Microscopy
3.04Å resolution

Cryo-EM structure of the human TRPC1/C4 heteromer

Released:
Source organism: Homo sapiens
Primary publication:
Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel.
Nat Struct Mol Biol (2024)
PMID: 39478185
Related structures: EMD-37718

Function and Biology Details

Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-281613 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Short transient receptor potential channel 1 Chain: A
Molecule details ›
Chain: A
Length: 797 amino acids
Theoretical weight: 91.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P48995 (Residues: 1-793; Coverage: 100%)
Gene names: TRP1, TRPC1
Sequence domains:
Short transient receptor potential channel 4 Chains: B, C, D
Molecule details ›
Chains: B, C, D
Length: 915 amino acids
Theoretical weight: 105.16 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9UBN4 (Residues: 1-977; Coverage: 91%)
  • Best match: Q9UBN4-2 (Residues: 1-893)
Gene name: TRPC4
Sequence domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.04Å
Relevant EMDB volumes: EMD-37718
Expression system: Homo sapiens