› 5hi9

Electron Microscopy
4.4Å resolution

Structure of the full-length TRPV2 channel by cryo-electron microscopy

Released:
DOI: 10.2210/pdb5hi9/pdb
PDB entry 5hi9 coloured by chain, front view.
PDB entry 5hi9 coloured by chain, side view.
PDB entry 5hi9 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of the full-length TRPV2 channel by cryo-EM.
Huynh KW, Cohen MR, Jiang J, Samanta A, Lodowski DT, Zhou ZH, Moiseenkova-Bell VY
OpenAccess logo Nat Commun 7 11130 (2016)
PMID: 27021073
Related structures: EMD-6618, EMD-6580

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-578063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transient receptor potential cation channel subfamily V member 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 770 amino acids
Theoretical weight: 87.67 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomycetales
UniProt:
  • Canonical: Q9WUD2 (Residues: 1-761; Coverage: 100%)
Gene names: Sac2b, Trpv2, Vrl1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.4Å
Relevant EMDB volumes: EMD-6580, EMD-6618
Expression system: Saccharomycetales

Quick links

Citations

36 review citations

Emerging Diversity in Lipid-Protein Interactions.
Corradi et al. (2019)
35 more

13 mentions without citation

Structural insights into the gating mechanisms of TRPV channels.
Pumroy et al. (2020)
12 more