› 4uxu

X-ray diffraction
1.71Å resolution

Crystal Structure of the Extracellular Domain of the Human Alpha9 Nicotinic Acetylcholine Receptor In Complex with Methyllycaconitine

Released:
DOI: 10.2210/pdb4uxu/pdb
PDB entry 4uxu coloured by chain, front view.
PDB entry 4uxu coloured by chain, side view.
PDB entry 4uxu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of free and antagonist-bound states of human α9 nicotinic receptor extracellular domain.
Zouridakis M, Giastas P, Zarkadas E, Chroni-Tzartou D, Bregestovski P, Tzartos SJ
Nat Struct Mol Biol 21 976-80 (2014)
PMID: 25282151

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193716 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuronal acetylcholine receptor subunit alpha-9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 25.31 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9UGM1 (Residues: 26-237; Coverage: 47%)
Gene names: CHRNA9, NACHRA9
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 MLK 2 x MLK
Ligand EPE 4 x EPE
Ligand EDO 3 x EDO
Ligand NA 2 x NA
Ligand NAG 4 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 63.434Å b: 66.246Å c: 75.191Å
α: 90° β: 102.76° γ: 90°
R-values:
R R work R free
0.211 0.206 0.235
Expression system: Komagataella pastoris

Quick links

Citations

17 review citations

Emerging Molecular Mechanisms of Signal Transduction in Pentameric Ligand-Gated Ion Channels.
Nemecz et al. (2016)
16 more

4 mentions without citation

Molecular interaction of α-conotoxin RgIA with the rat α9α10 nicotinic acetylcholine receptor.
Azam et al. (2015)
3 more