Crystal structure of ALPHA9 nachr extracellular domain in complex with alpha-conotoxin rgia

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 49% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 413 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan, 1 modified (disulfide, N-glycosylation, nonstandard).

Compared structures

• 6HY7 · Crystal structure of alpha9 nAChR extracellular domain in complex with alpha-conotoxin… · 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 A against A, TM-score 0.93
• P0C1D0 · AlphaFold monomer V2.0 prediction for alpha-conotoxin rgia (P0C1D0) · a predicted model of the same protein · chain B against A, TM-score 0.53

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
• Every structure of UniProt P0C1D0
• Elsewhere: RCSB PDB 6HY7 · PDBe 6HY7 · UniProt Q9UGM1 · UniProt P0C1D0