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PDBsum entry 4ey6

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protein ligands Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
4ey6
Jmol
Contents
Protein chain
530 a.a.
Ligands
FUC-NAG-NAG ×2
GNT ×2
EDO ×3
NAG
NO3 ×2
PE8
Waters ×385
PDB id:
4ey6
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of recombinant human acetylcholinesterase with (-)-galantamine
Structure: Acetylcholinesterase. Chain: a, b. Fragment: unp residues 33-574. Synonym: ache. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ache. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek-293
Resolution:
2.40Å     R-factor:   0.169     R-free:   0.206
Authors: J.Cheung,M.Rudolph,F.Burshteyn,M.Cassidy,E.Gary,J.Love,J.Hei M.Franklin
Key ref: J.Cheung et al. (2012). Structures of human acetylcholinesterase in complex with pharmacologically important ligands. J Med Chem, 55, 10282-10286. PubMed id: 23035744 DOI: 10.1021/jm300871x
Date:
01-May-12     Release date:   17-Oct-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P22303  (ACES_HUMAN) -  Acetylcholinesterase
Seq:
Struc:
 
Seq:
Struc:
614 a.a.
530 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.7  - Acetylcholinesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetylcholine + H2O = choline + acetate
Acetylcholine
Bound ligand (Het Group name = NAG)
matches with 41.18% similarity
+ H(2)O
= choline
+
acetate
Bound ligand (Het Group name = EDO)
matches with 60.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   18 terms 
  Biological process     small molecule metabolic process   29 terms 
  Biochemical function     carboxylic ester hydrolase activity     12 terms  

 

 
    reference    
 
 
DOI no: 10.1021/jm300871x J Med Chem 55:10282-10286 (2012)
PubMed id: 23035744  
 
 
Structures of human acetylcholinesterase in complex with pharmacologically important ligands.
J.Cheung, M.J.Rudolph, F.Burshteyn, M.S.Cassidy, E.N.Gary, J.Love, M.C.Franklin, J.J.Height.
 
  ABSTRACT  
 
Human acetylcholinesterase (AChE) is a significant target for therapeutic drugs. Here we present high resolution crystal structures of human AChE, alone and in complexes with drug ligands; donepezil, an Alzheimer's disease drug, binds differently to human AChE than it does to Torpedo AChE. These crystals of human AChE provide a more accurate platform for further drug development than previously available.