7l2h

Electron Microscopy
2.63Å resolution

Cryo-EM structure of unliganded full-length TRPV1 at neutral pH

Released:
Source organism: Rattus norvegicus
Primary publication:
Structural snapshots of TRPV1 reveal mechanism of polymodal functionality.
Cell 184 5138-5150.e12 (2021)
PMID: 34496225
Related structures: EMD-23128

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-128685 (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: 842 amino acids
Theoretical weight: 95.33 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: O35433 (Residues: 2-838; Coverage: 100%)
Gene names: Trpv1, Vr1, Vr1l
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.63Å
Relevant EMDB volumes: EMD-23128
Expression system: Homo sapiens