Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 a resolution

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 44% strand (DSSP).

Ligands and binding sites

• MAN · alpha-D-mannopyranose · sugar · 8 copies · chains B, A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 754 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

• 2QC1 · Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1… · the same entry in another collection · chain A against A, TM-score 1.00
• P60616 · AlphaFold monomer V2.0 prediction for alpha-bungarotoxin isoform V31 (P60616) · a predicted model of the same protein · chain A against A, TM-score 0.98
• P04756 · AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit alpha (P04756) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 P60616
• Every structure of UniProt P04756
• Elsewhere: RCSB PDB 2QC1 · PDBe 2QC1 · UniProt P60616 · UniProt P04756