Structure of mouse acetylcholinesterase complex with huprine derivative

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).

Ligands and binding sites

• H34 · (1-{4-[(7S,11S)-12-amino-3-chloro-6,7,10,11-tetrahydro-7,11-methanocycloocta[b]quinolin-9-yl]butyl}-1H-1,2,3-triazol-4-yl)methanol · ligand · 4 copies · chains A, B, C, D
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains B
• SO4 · Sulfate ion · ion · 14 copies · chains A, B, C, D
• CL · Chloride ion · ion · 5 copies · chains A, B, C

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• C–D · 980 Ų buried · 12 hydrogen bonds · protein-protein
• A–B · 977 Ų buried · 9 hydrogen bonds · protein-protein
• A–D · 589 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 554 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

• 4A16 · Structure of mouse Acetylcholinesterase complex with Huprine derivative · the same entry in another collection · chain D against D, TM-score 1.00
• P21836 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P21836) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P21836
• Elsewhere: RCSB PDB 4A16 · PDBe 4A16 · UniProt P21836