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PDBsum entry 2wls

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2wls
Jmol
Contents
Protein chains
535 a.a. *
Ligands
NAG ×2
X13 ×2
PEG
P6G
Waters ×349
* Residue conservation analysis
PDB id:
2wls
Name: Hydrolase
Title: Crystal structure of mus musculus acetylcholinesterase in complex with amts13
Structure: Acetylcholinesterase. Chain: a, b. Fragment: catalytic domain, residues 32-574. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293f.
Resolution:
2.60Å     R-factor:   0.185     R-free:   0.226
Authors: Y.P.Pang,F.Ekstrom,G.A.Polsinelli,Y.Gao,S.Rana,D.H.Hua, B.Andersson,P.O.Andersson,L.Peng,S.K.Singh,R.K.Mishra, K.Y.Zhu,A.M.Fallon,D.W.Ragsdale,S.Brimijoin
Date:
25-Jun-09     Release date:   08-Sep-09    
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 41.00% 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   17 terms 
  Biological process     synapse assembly   13 terms 
  Biochemical function     carboxylic ester hydrolase activity     9 terms