› 1ux2

X-ray diffraction
2.2Å resolution

X-ray structure of acetylcholine binding protein (AChBP)

Released:
DOI: 10.2210/pdb1ux2/pdb
PDB entry 1ux2 coloured by chain, front view.
PDB entry 1ux2 coloured by chain, side view.
PDB entry 1ux2 coloured by chain, top view.
Source organism: Lymnaea stagnalis
Primary publication:
Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures.
Celie PH, van Rossum-Fikkert SE, van Dijk WJ, Brejc K, Smit AB, Sixma TK
Neuron 41 907-14 (2004)
PMID: 15046723

Function and Biology Details

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

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: 212 amino acids
Theoretical weight: 24.12 KDa
Source organism: Lymnaea stagnalis
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P58154 (Residues: 18-229; Coverage: 100%)
Sequence domains: Neurotransmitter-gated ion-channel ligand binding domain
Structure domains: Neurotransmitter-gated ion-channel ligand-binding domain

Ligands and Environments

4 bound ligands:
Ligand EPE 8 x EPE
Ligand NAG 10 x NAG
Ligand SO4 2 x SO4
Ligand NH4 4 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41212
Unit cell:
a: 140.639Å b: 140.639Å c: 238.257Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.236 0.284
Expression system: Komagataella pastoris

Quick links

Citations

96 review citations

Mammalian nicotinic acetylcholine receptors: from structure to function.
Albuquerque et al. (2009)
95 more

12 mentions without citation

Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations.
Hansen et al. (2005)
11 more