› 6g8z

Electron Microscopy
3.66Å resolution

Structure of the pore domain of homomeric mLRRC8A volume-regulated anion channel at 3.66 A resolution

Released:
DOI: 10.2210/pdb6g8z/pdb
PDB entry 6g8z coloured by chain, front view.
PDB entry 6g8z coloured by chain, side view.
PDB entry 6g8z coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure of a volume-regulated anion channel of the LRRC8 family.
Deneka D, Sawicka M, Lam AKM, Paulino C, Dutzler R
Nature 558 254-259 (2018)
PMID: 29769723
Related structures: EMD-4362

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182395 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Volume-regulated anion channel subunit LRRC8A Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 810 amino acids
Theoretical weight: 94.24 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q80WG5 (Residues: 1-810; Coverage: 100%)
Gene names: Lrrc8, Lrrc8a
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.66Å
Relevant EMDB volumes: EMD-4362
Expression system: Homo sapiens

Quick links

Citations

25 review citations

Cell Volume-Activated and Volume-Correlated Anion Channels in Mammalian Cells: Their Biophysical, Molecular, and Pharmacological Properties.
Okada et al. (2019)
24 more

3 mentions without citation

On the molecular nature of large-pore channels.
Syrjanen et al. (2021)
2 more