› 2wnj

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF APLYSIA ACHBP IN COMPLEX WITH DMXBA

Released:
DOI: 10.2210/pdb2wnj/pdb
PDB entry 2wnj coloured by chain, front view.
PDB entry 2wnj coloured by chain, side view.
PDB entry 2wnj coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine receptor.
Hibbs RE, Sulzenbacher G, Shi J, Talley TT, Conrod S, Kem WR, Taylor P, Marchot P, Bourne Y
EMBO J 28 3040-51 (2009)
PMID: 19696737

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
Macromolecules (2 distinct):
Neurotransmitter-gated ion-channel ligand-binding domain-containing protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
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

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
2 bound ligands:
Ligand ZY7 5 x ZY7
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 87.222Å b: 114.799Å c: 131.284Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.206
Expression system: Homo sapiens

Quick links

Citations

14 review citations

The structural basis of function in Cys-loop receptors.
Thompson et al. (2010)
13 more

10 mentions without citation

Size matters in activation/inhibition of ligand-gated ion channels.
Du et al. (2012)
9 more