› 2yme

X-ray diffraction
2.4Å resolution

Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with granisetron

Released:
DOI: 10.2210/pdb2yme/pdb
PDB entry 2yme coloured by chain, front view.
PDB entry 2yme coloured by chain, side view.
PDB entry 2yme coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Structural basis of ligand recognition in 5-HT3 receptors.
Kesters D, Thompson AJ, Brams M, van Elk R, Spurny R, Geitmann M, Villalgordo JM, Guskov A, Danielson UH, Lummis SC, Smit AB, Ulens C
EMBO Rep 14 49-56 (2013)
PMID: 23196367

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: 205 amino acids
Theoretical weight: 23.34 KDa
Source organism: Aplysia californica
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q8WSF8 (Residues: 20-224; Coverage: 95%)
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 NAG 9 x NAG
Ligand CWB 10 x CWB
Ligand PO4 5 x PO4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 83.09Å b: 138.9Å c: 119.89Å
α: 90° β: 91.07° γ: 90°
R-values:
R R work R free
0.172 0.17 0.226
Expression system: Spodoptera frugiperda

Quick links

Citations

15 review citations

Biophysics in drug discovery: impact, challenges and opportunities.
Renaud et al. (2016)
14 more

2 mentions without citation

The muscarinic antagonists scopolamine and atropine are competitive antagonists at 5-HT3 receptors.
Lochner et al. (2016)
1 more