PDBe 3j5r

Electron Microscopy
4.2Å resolution

Reconstruction of TRPV1 ion channel in complex with capsaicin by single particle cryo-microscopy

Released:
Source organism: Rattus norvegicus
Primary publication:
TRPV1 structures in distinct conformations reveal activation mechanisms.
OpenAccess logo Nature 504 113-8 (2013)
PMID: 24305161
Related structures: EMD-5777

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: O35433 (Residues: 111-719; Coverage: 70%)
Gene names: Trpv1, Vr1, Vr1l
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.2Å
Relevant EMDB volumes: EMD-5777
Expression system: Homo sapiens