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PDBsum entry 2xuh

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2xuh
Jmol
Contents
Protein chains
537 a.a. *
Ligands
TZ4 ×2
Waters ×72
* Residue conservation analysis
PDB id:
2xuh
Name: Hydrolase
Title: Crystal structure of mache-y337a-tz2pa6 anti complex (10 mth
Structure: Acetylcholinesterase. Chain: a, b. Fragment: catalytic domain, residues 32-574. Synonym: ache. Engineered: yes. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: black6cba cross f1. Organ: brain (cdna). Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293. Other_details: lambda-fix cdna, genomic DNA
Resolution:
2.65Å     R-factor:   0.198     R-free:   0.245
Authors: Y.Bourne,Z.Radic,P.Taylor,P.Marchot
Key ref: Y.Bourne et al. (2010). Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state. J Am Chem Soc, 132, 18292-18300. PubMed id: 21090615
Date:
19-Oct-10     Release date:   08-Dec-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21836  (ACES_MOUSE) -  Acetylcholinesterase
Seq:
Struc:
 
Seq:
Struc:
614 a.a.
537 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
+ 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    
 
 
J Am Chem Soc 132:18292-18300 (2010)
PubMed id: 21090615  
 
 
Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state.
Y.Bourne, Z.Radić, P.Taylor, P.Marchot.
 
  ABSTRACT  
 
No abstract given.