GL1X · GenesisL1 explorer

Research workbench

Update of native acetylcholinesterase from drosophila melanogaster

Analyse Update of native acetylcholinesterase from drosophila melanogaster in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XYS
Type
protein
Length
535 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetylcholinesterase
EC
3.1.1.7
UniProt
P07140
Ligands
NAG, MAN, BMA, CL
Pockets
3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetylcholinesterase (EC 3.1.1.7)protein53538% helix, 16% strandP07140

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · chains A
  • CL · Chloride ion · ion · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11760.710.8928empty
21600.550.8127empty
33080.550.7540empty

Modifications

Observed in the structure: 3 disulfide, 1 covalent, 1 glycan (disulfide, additive adduct, N-glycosylation).

Compared structures

  • 6XYS · Update of native acetylcholinesterase from Drosophila Melanogaster · the same entry in another collection · chain A against A, TM-score 1.00
  • P07140 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P07140) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.