› 5oal

X-ray diffraction
3.2Å resolution

Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S, G162E)

Released:
DOI: 10.2210/pdb5oal/pdb
PDB entry 5oal coloured by chain, front view.
PDB entry 5oal coloured by chain, side view.
PDB entry 5oal coloured by chain, top view.
Source organism: Aplysia californica
Primary publication:
Engineering a surrogate human heteromeric α/β glycine receptor orthosteric site exploiting the structural homology and stability of acetylcholine-binding protein.
Dawson A, Trumper P, de Souza JO, Parker H, Jones MJ, Hales TG, Hunter WN
OpenAccess logo IUCrJ 6 1014-1023 (2019)
PMID: 31709057

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, K, L, M, N, O
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 249 amino acids
Theoretical weight: 28.36 KDa
Source organism: Aplysia californica
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q8WSF8 (Residues: 1-236; Coverage: 100%)
Sequence domains: Neurotransmitter-gated ion-channel ligand binding domain
Structure domains: Neurotransmitter-gated ion-channel ligand-binding domain

Ligands and Environments

2 bound ligands:
Ligand SY9 15 x SY9
Ligand ARG 1 x ARG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P32
Unit cell:
a: 130.9Å b: 130.9Å c: 190.139Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.231
Expression system: Spodoptera frugiperda

Quick links

Citations

5 citation in other articles

A Structural Rationale for N-Methylbicuculline Acting as a Promiscuous Competitive Antagonist of Inhibitory Pentameric Ligand-Gated Ion Channels.
Jones et al. (2020)
4 more

1 mention without citation

Engineering a surrogate human heteromeric α/β glycine receptor orthosteric site exploiting the structural homology and stability of acetylcholine-binding protein.
Dawson et al. (2019)