Electron Microscopy
3.28Å resolution

Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy

Source organism: Rattus norvegicus
Primary publication:
Structure of the TRPV1 ion channel determined by electron cryo-microscopy.
Nature 504 107-12 (2013)
PMID: 24305160
Related structures: EMD-5778

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Transient receptor potential cation channel subfamily V member 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 598 amino acids
Theoretical weight: 68.24 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
  • Canonical: O35433 (Residues: 111-719; Coverage: 70%)
Gene names: Trpv1, Vr1, Vr1l
Sequence domains:
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.275Å
Relevant EMDB volumes: EMD-5778
Expression system: Homo sapiens