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PDBsum entry 4arb

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protein ligands links
Hydrolase PDB id
4arb
Jmol
Contents
Protein chains
535 a.a.
Ligands
C57 ×2
PEG ×6
NAG ×3
P6G
Waters ×989
PDB id:
4arb
Name: Hydrolase
Title: Mus musculus acetylcholinesterase in complex with (s)-c5685 resolution.
Structure: Acetylcholinesterase. Chain: a, b. Fragment: catalytic domain, residues 32-574. Synonym: ache. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_variant: hek293f
Resolution:
2.25Å     R-factor:   0.172     R-free:   0.209
Authors: L.Berg,M.S.Niemiec,W.Qian,C.D.Andersson,P.Wittungstafshede,F A.Linusson
Key ref: L.Berg et al. (2012). Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase. Angew Chem Int Ed Engl, 51, 12716-12720. PubMed id: 23161758
Date:
23-Apr-12     Release date:   28-Nov-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21836  (ACES_MOUSE) -  Acetylcholinesterase
Seq:
Struc:
 
Seq:
Struc:
614 a.a.
535 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
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   12 terms 
  Biological process     cell adhesion   9 terms 
  Biochemical function     carboxylic ester hydrolase activity     10 terms  

 

 
    reference    
 
 
Angew Chem Int Ed Engl 51:12716-12720 (2012)
PubMed id: 23161758  
 
 
Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase.
L.Berg, M.S.Niemiec, W.Qian, C.D.Andersson, P.Wittung-Stafshede, F.Ekström, A.Linusson.
 
  ABSTRACT  
 
Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated that the enantiomers exhibit different thermodynamic profiles. Analyses of the noncovalent interactions in the protein-ligand complexes revealed that these differences are partly due to nonclassical hydrogen bonds between the ligands and aromatic side chains of the protein.