› 3zdh

X-ray diffraction
2.2Å resolution

Crystal structure of Ls-AChBP complexed with carbamoylcholine analogue N,N-dimethyl-4-(1-methyl-1H-imidazol-2-yloxy)butan-2-amine

Released:
DOI: 10.2210/pdb3zdh/pdb
PDB entry 3zdh coloured by chain, front view.
PDB entry 3zdh coloured by chain, side view.
PDB entry 3zdh coloured by chain, top view.
Source organism: Lymnaea stagnalis
Primary publication:
Synthesis, pharmacology, and biostructural characterization of novel α4β2 nicotinic acetylcholine receptor agonists.
Ussing CA, Hansen CP, Petersen JG, Jensen AA, Rohde LA, Ahring PK, Nielsen EØ, Kastrup JS, Gajhede M, Frølund B, Balle T
J Med Chem 56 940-51 (2013)
PMID: 23256554

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
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 210 amino acids
Theoretical weight: 23.86 KDa
Source organism: Lymnaea stagnalis
Expression system: Spodoptera frugiperda
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

3 bound ligands:
Ligand XRS 10 x XRS
Ligand SO4 2 x SO4
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21212
Unit cell:
a: 137.334Å b: 143.822Å c: 115.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.245
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Structural Studies of Nicotinic Acetylcholine Receptors: Using Acetylcholine-Binding Protein as a Structural Surrogate.
Shahsavar et al. (2016)
1 more

1 mention without citation

Structural mechanisms for α-conotoxin activity at the human α3β4 nicotinic acetylcholine receptor.
Abraham et al. (2017)