spacer
spacer

PDBsum entry 2y1k

Go to PDB code: 
protein ligands metals links
Hydrolase PDB id
2y1k
Jmol
Contents
Protein chain
525 a.a.
Ligands
SO4 ×5
GOL
NAG-FUC
NAG ×7
FU4 ×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. Other_details:
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:   0.184     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 DOI: 10.1021/tx100447k
Date:
08-Dec-10     Release date:   29-Jun-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06276  (CHLE_HUMAN) -  Cholinesterase
Seq:
Struc:
 
Seq:
Struc:
602 a.a.
525 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 = choline + a carboxylate
acylcholine
+ H(2)O
= choline
+ carboxylate
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   12 terms 
  Biochemical function     catalytic activity     9 terms  

 

 
    reference    
 
 
DOI no: 10.1021/tx100447k 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.