› 7t6n

Electron Microscopy
2.9Å resolution

Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 2

Released:
DOI: 10.2210/pdb7t6n/pdb
PDB entry 7t6n coloured by chain, front view.
PDB entry 7t6n coloured by chain, side view.
PDB entry 7t6n coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structural basis of TRPV5 regulation by physiological and pathophysiological modulators.
Fluck EC, Yazici AT, Rohacs T, Moiseenkova-Bell VY
OpenAccess logo Cell Rep 39 110737 (2022)
PMID: 35476976
Related structures: EMD-25720

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-195036 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transient receptor potential cation channel subfamily V member 5 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 739 amino acids
Theoretical weight: 83.78 KDa
Source organism: Oryctolagus cuniculus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q9XSM3 (Residues: 1-730; Coverage: 100%)
Gene names: Ecac1, Trpv5
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-25720
Expression system: Saccharomyces cerevisiae

Quick links

Citations

4 review citations

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

1 mention without citation

Structural basis of TRPV5 regulation by physiological and pathophysiological modulators.
Fluck et al. (2022)