Crystal structure of a chimeric acetylcholine binding protein from aplysia californica (ac-achbp) containing loop C from the human alpha 3 nicotinic acetylcholine receptor in complex with cytisine

Structure

x-ray diffraction · 5 distinct chains · 10% helix, 52% strand (DSSP).

Ligands and binding sites

• C5E · (1R,5S)-1,2,3,4,5,6-hexahydro-8H-1,5-methanopyrido[1,2-a][1,5]diazocin-8-one · ligand · 2 copies · chains B, C, D, E

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

Pockets

19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• B–C · 1347 Ų buried · 21 hydrogen bonds · protein-protein
• D–E · 1340 Ų buried · 17 hydrogen bonds · protein-protein
• A–E · 1270 Ų buried · 16 hydrogen bonds · protein-protein
• A–B · 1213 Ų buried · 15 hydrogen bonds · protein-protein
• C–D · 1152 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

• 5SYO · Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica… · the same entry in another collection · chain E against E, TM-score 1.00
• P32297 · AlphaFold monomer V2.0 prediction for neuronal acetylcholine receptor subunit alpha-3… · a predicted model of the same protein · chain C against A, TM-score 0.92

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 Q8WSF8
• Every structure of UniProt P32297
• Elsewhere: RCSB PDB 5SYO · PDBe 5SYO · UniProt Q8WSF8 · UniProt P32297