4aq5

Electron Microscopy
6.2Å resolution

Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class)

Released:
Source organism: Torpedo marmorata
Primary publication:
Gating movement of acetylcholine receptor caught by plunge-freezing.
J Mol Biol 422 617-634 (2012)
PMID: 22841691
Related structures: EMD-2071

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-136096 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Acetylcholine receptor subunit alpha Chains: A, D
Molecule details ›
Chains: A, D
Length: 461 amino acids
Theoretical weight: 52.85 KDa
Source organism: Torpedo marmorata
UniProt:
  • Canonical: P02711 (Residues: 1-461; Coverage: 100%)
Gene name: CHRNA1
Sequence domains:
Acetylcholine receptor subunit beta Chain: B
Molecule details ›
Chain: B
Length: 493 amino acids
Theoretical weight: 56.12 KDa
Source organism: Torpedo marmorata
UniProt:
  • Canonical: Q6S3I0 (Residues: 1-493; Coverage: 100%)
Sequence domains:
Acetylcholine receptor subunit delta Chain: C
Molecule details ›
Chain: C
Length: 522 amino acids
Theoretical weight: 60.02 KDa
Source organism: Torpedo marmorata
UniProt:
  • Canonical: Q6S3H8 (Residues: 1-522; Coverage: 100%)
Sequence domains:
Acetylcholine receptor gamma subunit Chain: E
Molecule details ›
Chain: E
Length: 488 amino acids
Theoretical weight: 56.23 KDa
Source organism: Torpedo marmorata
UniProt:
  • Canonical: Q6S3H9 (Residues: 18-505; Coverage: 100%)
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 6.2Å
Relevant EMDB volumes: EMD-2071