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PDBsum entry 4a16

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4a16
Jmol
Contents
Protein chains
541 a.a.
Ligands
H34 ×4
SO4 ×14
NAG
Metals
_CL ×5
Waters ×2323
PDB id:
4a16
Name: Hydrolase
Title: Structure of mouse acetylcholinesterase complex with huprine derivative
Structure: Acetylcholinesterase. Chain: a, b, c, d. Fragment: residues 35-574. Synonym: ache. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: cho-k1.
Resolution:
2.65Å     R-factor:   0.156     R-free:   0.205
Authors: E.Carletti,J.P.Colletier,F.Nachon,M.Weik,C.Ronco,L.Jean,P.Y.
Key ref: C.Ronco et al. (2012). Huprine derivatives as sub-nanomolar human acetylcholinesterase inhibitors: from rational design to validation by X-ray crystallography. ChemMedChem, 7, 400-405. PubMed id: 22052791
Date:
14-Sep-11     Release date:   28-Mar-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21836  (ACES_MOUSE) -  Acetylcholinesterase
Seq:
Struc:
 
Seq:
Struc:
614 a.a.
541 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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   17 terms 
  Biological process     synapse assembly   13 terms 
  Biochemical function     carboxylic ester hydrolase activity     9 terms  

 

 
    reference    
 
 
ChemMedChem 7:400-405 (2012)
PubMed id: 22052791  
 
 
Huprine derivatives as sub-nanomolar human acetylcholinesterase inhibitors: from rational design to validation by X-ray crystallography.
C.Ronco, E.Carletti, J.P.Colletier, M.Weik, F.Nachon, L.Jean, P.Y.Renard.
 
  ABSTRACT  
 
No abstract given.