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PDBsum entry 4aqd

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4aqd
Jmol
Contents
Protein chain
527 a.a.
Ligands
BAL ×2
NAG-NAG ×2
NAG-NAG-FUL ×6
NAG ×6
NAG-NAG-MAN
PG4 ×2
EDO ×19
UNX-UNX
UNX ×8
GLY ×2
PEG ×2
Metals
_CL
Waters ×278
PDB id:
4aqd
Name: Hydrolase
Title: Crystal structure of fully glycosylated human butyrylcholine
Structure: Butyrylcholinesterase. Chain: a, b. Fragment: residues 27-557. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Expression_system_cell_line: s2.
Resolution:
2.50Å     R-factor:   0.165     R-free:   0.232
Authors: X.Brazzolotto,M.Wandhammer,C.Ronco,M.Trovaslet,L.Jean,O.Lock P.Y.Renard,F.Nachon
Key ref: X.Brazzolotto et al. (2012). Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure. FEBS J, 279, 2905-2916. PubMed id: 22726956
Date:
16-Apr-12     Release date:   04-Jul-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P06276  (CHLE_HUMAN) -  Cholinesterase
Seq:
Struc:
 
Seq:
Struc:
602 a.a.
527 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.8  - Cholinesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An acylcholine + H2O = choline + a carboxylate
acylcholine
+ H(2)O
=
choline
Bound ligand (Het Group name = GLY)
matches with 50.00% similarity
+
carboxylate
Bound ligand (Het Group name = BAL)
matches with 42.86% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   7 terms 
  Biological process     response to drug   13 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
FEBS J 279:2905-2916 (2012)
PubMed id: 22726956  
 
 
Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure.
X.Brazzolotto, M.Wandhammer, C.Ronco, M.Trovaslet, L.Jean, O.Lockridge, P.Y.Renard, F.Nachon.
 
  ABSTRACT  
 
No abstract given.