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MolNFT v1 · #8479 · protein

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)- (-)-BIS(12)-hupyridone at 2.15A resolution

1H23: “Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)- (-)-BIS(12)-hupyridone at 2.15A…”. X-ray diffraction, 2 ligands (E12, NAG), 4 pockets (best druggability 0.76). MolNFT v1 #8479 on GenesisL1: 3D structure…

PDB
1H23
Type
protein
Length
528 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetylcholinesterase
EC
3.1.1.7
UniProt
P04058
Ligands
E12, NAG
Pockets
4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetylcholinesterase (EC 3.1.1.7)protein52839% helix, 17% strandP04058

Ligands and binding sites

  • E12 · (S,S)-(-)-N,N'-di-5'-[5',6',7',8'-tetrahydro- 2'(1'H)-quinolynyl]-1,12-diaminododecane dihydrochloride · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13390.760.8737E12
23130.560.7634empty
31240.460.7715empty
4500.310.7713empty

Modifications

Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 1H23 · Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P04058 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P04058) · a predicted model of the same protein · chain A against A, TM-score 1.00

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