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 (E,2S)-N-methyl-5- (5-phenoxy-3-PYRIDYL)PENT-4-en-2-amine (ti-5312)

Structure

x-ray diffraction · 5 distinct chains · 11% helix, 51% strand (DSSP).

Ligands and binding sites

• 7LB · (E,2S)-N-methyl-5-(5-phenoxy-3-pyridyl)pent-4-en-2-amine · ligand · 4 copies · chains A, B, C, D, E
• SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E
• 1PE · Pentaethylene glycol · additive · chains A, E

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

Pockets

15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• D–E · 1426 Ų buried · 18 hydrogen bonds · protein-protein
• A–B · 1364 Ų buried · 18 hydrogen bonds · protein-protein
• A–E · 1327 Ų buried · 19 hydrogen bonds · protein-protein
• C–D · 1263 Ų buried · 14 hydrogen bonds · protein-protein
• B–C · 1195 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

• 5TVC · 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 E against A, TM-score 0.90

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 5TVC · PDBe 5TVC · UniProt Q8WSF8 · UniProt P32297