› 2wzy

X-ray diffraction
2.51Å resolution

Crystal structure of A-AChBP in complex with 13-desmethyl spirolide C

Released:
DOI: 10.2210/pdb2wzy/pdb
PDB entry 2wzy coloured by chain, front view.
PDB entry 2wzy coloured by chain, side view.
PDB entry 2wzy coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism.
Bourne Y, Radic Z, Aráoz R, Talley TT, Benoit E, Servent D, Taylor P, Molgó J, Marchot P
Proc Natl Acad Sci U S A 107 6076-81 (2010)
PMID: 20224036

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, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 228 amino acids
Theoretical weight: 25.97 KDa
Source organism: Aplysia californica
Expression system: Homo sapiens
UniProt:
  • Canonical: Q8WSF8 (Residues: 16-236; Coverage: 100%)
Sequence domains: Neurotransmitter-gated ion-channel ligand binding domain
Structure domains: Neurotransmitter-gated ion-channel ligand-binding domain

Ligands and Environments

1 bound ligand:
Ligand SQX 10 x SQX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 77.626Å b: 131.748Å c: 125.593Å
α: 90° β: 90.42° γ: 90°
R-values:
R R work R free
0.177 0.176 0.237
Expression system: Homo sapiens

Quick links

Citations

15 review citations

Emerging Molecular Mechanisms of Signal Transduction in Pentameric Ligand-Gated Ion Channels.
Nemecz et al. (2016)
14 more

9 mentions without citation

Cyclic imine toxins from dinoflagellates: a growing family of potent antagonists of the nicotinic acetylcholine receptors.
Molgó et al. (2017)
8 more