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PDBsum entry 2y1k

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protein ligands metals links
Hydrolase PDB id
2y1k

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
526 a.a.
Ligands
NAG-FUC
SO4 ×5
GOL
NAG ×7
FUC ×2
Metals
_NA
_CL
Waters ×229
PDB id:
2y1k
Name: Hydrolase
Title: Structure of human butyrylcholinesterase inhibited by cbdp (12h soak): phosphoserine adduct
Structure: Cholinesterase. Chain: a. Fragment: residues 29-557. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: cho-k1.
Resolution:
2.50Å     R-factor:   0.185     R-free:   0.247
Authors: E.Carletti,J.P.Colletier,F.Nachon,M.Weik
Key ref: E.Carletti et al. (2011). Reaction of cresyl saligenin phosphate, the organophosphorus agent implicated in aerotoxic syndrome, with human cholinesterases: mechanistic studies employing kinetics, mass spectrometry, and X-ray structure analysis. Chem Res Toxicol, 24, 797-808. PubMed id: 21438623
Date:
08-Dec-10     Release date:   29-Jun-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06276  (CHLE_HUMAN) -  Cholinesterase from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
602 a.a.
526 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.8  - cholinesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: an acylcholine + H2O = a carboxylate + choline + H+
acylcholine
+ H2O
= carboxylate
+ choline
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Chem Res Toxicol 24:797-808 (2011)
PubMed id: 21438623  
 
 
Reaction of cresyl saligenin phosphate, the organophosphorus agent implicated in aerotoxic syndrome, with human cholinesterases: mechanistic studies employing kinetics, mass spectrometry, and X-ray structure analysis.
E.Carletti, L.M.Schopfer, J.P.Colletier, M.T.Froment, F.Nachon, M.Weik, O.Lockridge, P.Masson.
 
  ABSTRACT  
 
No abstract given.

 

 

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