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PDBsum entry 4b81

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
4b81
Jmol
Contents
Protein chains
535 a.a.
Ligands
P6G
ZN4 ×2
SO4 ×2
NAG ×3
PEG ×8
Waters ×180
PDB id:
4b81
Name: Hydrolase
Title: Mus musculus acetylcholinesterase in complex with 1-(4-chloro-phenyl)-n-(2-diethylamino-ethyl)-methanesulfona
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_cell_line: hek 293f.
Resolution:
2.80Å     R-factor:   0.197     R-free:   0.239
Authors: C.D.Andersson,N.Forsgren,C.Akfur,A.Allgardsson,L.Berg,W.Qian F.Ekstrom,A.Linusson
Key ref: C.D.Andersson et al. (2013). Divergent structure-activity relationships of structurally similar acetylcholinesterase inhibitors. J Med Chem, 56, 7615-7624. PubMed id: 23984975 DOI: 10.1021/jm400990p
Date:
24-Aug-12     Release date:   04-Sep-13    
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    
 
 
DOI no: 10.1021/jm400990p J Med Chem 56:7615-7624 (2013)
PubMed id: 23984975  
 
 
Divergent structure-activity relationships of structurally similar acetylcholinesterase inhibitors.
C.D.Andersson, N.Forsgren, C.Akfur, A.Allgardsson, L.Berg, C.Engdahl, W.Qian, F.Ekström, A.Linusson.
 
  ABSTRACT  
 
No abstract given.