spacer
spacer

PDBsum entry 2xuf

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2xuf
Jmol
Contents
Protein chains
534 a.a. *
Ligands
NAG ×2
P6G
TZ4 ×2
Waters ×256
* Residue conservation analysis
PDB id:
2xuf
Name: Hydrolase
Title: Crystal structure of mache-y337a-tz2pa6 anti complex (1 mth)
Structure: Acetylcholinesterase. Chain: a, b. Fragment: catalytic domain, residues 32-575. 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. Other_details: lambda-fix cdna, genomic DNA
Resolution:
2.55Å     R-factor:   0.191     R-free:   0.220
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
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21836  (ACES_MOUSE) -  Acetylcholinesterase
Seq:
Struc:
 
Seq:
Struc:
614 a.a.
534 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 41.00% 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    
 
 
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.