PDBe 3j5q

Electron Microscopy
3.8Å resolution

Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy

Released:
Primary publication:
TRPV1 structures in distinct conformations reveal activation mechanisms.
OpenAccess logo Nature 504 113-8 (2013)
PMID: 24305161
Related structures: EMD-5776

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transient receptor potential cation channel subfamily V member 1 Chains: B, D, E, G
Molecule details ›
Chains: B, D, E, G
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:
Structure domains: Ankyrin repeat-containing domain
Double-knot toxin Chains: A, C, F, H
Molecule details ›
Chains: A, C, F, H
Length: 31 amino acids
Theoretical weight: 2.66 KDa
Source organism: Chilobrachys guangxiensis

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-5776
Expression system: Homo sapiens