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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   12 terms 
  Biological process     cell adhesion   9 terms 
  Biochemical function     carboxylic ester hydrolase activity     10 terms