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› 4bqt

X-ray diffraction
2.88Å resolution

Aplysia californica AChBP in complex with Cytisine

Released:
DOI: 10.2210/pdb4bqt/pdb
Model geometry
Fit model/data
PDB entry 4bqt coloured by chain, front view.
PDB entry 4bqt coloured by chain, side view.
PDB entry 4bqt coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Structural characterization of binding mode of smoking cessation drugs to nicotinic acetylcholine receptors through study of ligand complexes with acetylcholine-binding protein.
Rucktooa P, Haseler CA, van Elk R, Smit AB, Gallagher T, Sixma TK
OpenAccess logo J Biol Chem 287 23283-93 (2012)
PMID: 22553201

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-186694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neurotransmitter-gated ion-channel ligand-binding domain-containing protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 217 amino acids
Theoretical weight: 24.69 KDa
Source organism: Aplysia californica
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q8WSF8 (Residues: 20-236; 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 C5E 5 x C5E
Ligand CL 11 x CL
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: I23
Unit cell:
a: 206.689Å b: 206.689Å c: 206.689Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.224
Expression system: Spodoptera frugiperda

Quick links

Citations

8 review citations

Structural insights into Cys-loop receptor function and ligand recognition.
Nys et al. (2013)
7 more

6 mentions without citation

Acetylation promotes TyrRS nuclear translocation to prevent oxidative damage.
Cao et al. (2017)
5 more