› 2pgz

X-ray diffraction
1.76Å resolution

Crystal structure of Cocaine bound to an ACh-Binding Protein

Released:
DOI: 10.2210/pdb2pgz/pdb
PDB entry 2pgz coloured by chain, front view.
PDB entry 2pgz coloured by chain, side view.
PDB entry 2pgz coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Galanthamine and non-competitive inhibitor binding to ACh-binding protein: evidence for a binding site on non-alpha-subunit interfaces of heteromeric neuronal nicotinic receptors.
Hansen SB, Taylor P
J Mol Biol 369 895-901 (2007)
PMID: 17481657

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: 230 amino acids
Theoretical weight: 26.21 KDa
Source organism: Aplysia californica
Expression system: Homo sapiens
UniProt:
  • Canonical: Q8WSF8 (Residues: 18-236; 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
3 bound ligands:
Ligand COC 2 x COC
Ligand NAG 1 x NAG
Ligand PG4 3 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1, APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 86.822Å b: 115.589Å c: 130.879Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.21
Expression system: Homo sapiens

Quick links

Citations

23 review citations

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

18 mentions without citation

Positive allosteric modulators as an approach to nicotinic acetylcholine receptor-targeted therapeutics: advantages and limitations.
Williams et al. (2011)
17 more