Crystal structure of the extracellular domain of the human ALPHA9 nicotinic acetylcholine receptor in complex with methyllycaconitine

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 52% strand (DSSP).

Ligands and binding sites

• MLK · Methyllycaconitine · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
• NA · Sodium ion · metal · 2 copies · chains A, B
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 4 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 543 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

• 4UXU · Crystal Structure of the Extracellular Domain of the Human Alpha9 Nicotinic Acetylcholine… · the same entry in another collection · chain A against A, TM-score 1.00
• Q9UGM1 · AlphaFold monomer V2.0 prediction for neuronal acetylcholine receptor subunit alpha-9… · a predicted model of the same protein · chain B against A, TM-score 0.93

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q9UGM1
• Elsewhere: RCSB PDB 4UXU · PDBe 4UXU · UniProt Q9UGM1