› 2xz5

X-ray diffraction
2.8Å resolution

MMTS-modified Y53C mutant of Aplysia AChBP in complex with acetylcholine

Released:
DOI: 10.2210/pdb2xz5/pdb
PDB entry 2xz5 coloured by chain, front view.
PDB entry 2xz5 coloured by chain, side view.
PDB entry 2xz5 coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Crystal structures of a cysteine-modified mutant in loop D of acetylcholine-binding protein.
Brams M, Gay EA, Sáez JC, Guskov A, van Elk R, van der Schors RC, Peigneur S, Tytgat J, Strelkov SV, Smit AB, Yakel JL, Ulens C
J Biol Chem 286 4420-8 (2011)
PMID: 21115477

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: 24.67 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

5 bound ligands:
Ligand ACH 10 x ACH
Ligand CL 5 x CL
Ligand PO4 10 x PO4
Ligand MPD 7 x MPD
Ligand NAG 2 x NAG
1 modified residue:
Ligand SCH 5 x SCH

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2221
Unit cell:
a: 82.123Å b: 119.405Å c: 267.744Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.219
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

Structure and pharmacology of pentameric receptor channels: from bacteria to brain.
Corringer et al. (2012)
4 more

7 mentions without citation

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