› 7mze

Electron Microscopy
3.42Å resolution

Cryo-EM structure of minimal TRPV1 with 2 bound RTX in opposite pockets

Released:
DOI: 10.2210/pdb7mze/pdb
PDB entry 7mze coloured by chain, front view.
PDB entry 7mze coloured by chain, side view.
PDB entry 7mze coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structural snapshots of TRPV1 reveal mechanism of polymodal functionality.
Zhang K, Julius D, Cheng Y
Cell 184 5138-5150.e12 (2021)
PMID: 34496225
Related structures: EMD-24091

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
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: 637 amino acids
Theoretical weight: 73.02 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: O35433 (Residues: 110-764; Coverage: 75%)
Gene names: Trpv1, Vr1, Vr1l
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand XJ7 2 x XJ7
Ligand NA 1 x NA
Ligand 6EU 2 x 6EU
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.42Å
Relevant EMDB volumes: EMD-24091
Expression system: Homo sapiens

Quick links

Citations

27 review citations

TRP (transient receptor potential) ion channel family: structures, biological functions and therapeutic interventions for diseases.
Zhang et al. (2023)
26 more

3 mentions without citation

Ligand-Binding Sites in Vanilloid-Subtype TRP Channels.
Yelshanskaya et al. (2022)
2 more