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X-ray diffraction
2.68Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholine-binding protein Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 210 amino acids
Theoretical weight: 23.86 KDa
Source organism: Lymnaea stagnalis
UniProt:
  • Canonical: P58154 (Residues: 20-229; Coverage: 100%)
Sequence domains: Neurotransmitter-gated ion-channel ligand binding domain
Structure domains: Neurotransmitter-gated ion-channel ligand-binding domain

Ligands and Environments

7 bound ligands:
Ligand 1PE 8 x 1PE
Ligand NAG 2 x NAG
Ligand SO4 20 x SO4
Ligand ACT 12 x ACT
Ligand NSE 6 x NSE
Ligand CL 4 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: C2
Unit cell:
a: 231.726Å b: 140.381Å c: 119.545Å
α: 90° β: 89.98° γ: 90°
R-values:
R R work R free
0.208 0.207 0.24

Quick links

Citations

8 review citations

Allosteric modulation of nicotinic acetylcholine receptors.
Chatzidaki et al. (2015)
7 more

1 mention without citation

Structural and functional studies of the modulator NS9283 reveal agonist-like mechanism of action at α4β2 nicotinic acetylcholine receptors.
Olsen et al. (2014)