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PDBsum entry 3o9m

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3o9m
Jmol
Contents
Protein chain
531 a.a.
Ligands
BEZ ×2
Waters ×2
PDB id:
3o9m
Name: Hydrolase
Title: Co-crystallization studies of full length recombinant bche w cocaine offers insights into cocaine detoxification
Structure: Cholinesterase. Chain: a, b. Synonym: acylcholine acylhydrolase, choline esterase ii, butyrylcholine esterase, pseudocholinesterase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: bche, che1. Expressed in: cricetulus griseus. Expression_system_taxid: 10029
Resolution:
2.98Å     R-factor:   0.225     R-free:   0.262
Authors: O.A.Asojo,M.N.Ngamelue,K.Homma,O.Lockridge
Key ref: O.A.Asojo et al. (2011). Cocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaine. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 434-437. PubMed id: 21505234 DOI: 10.1107/S1744309111004805
Date:
04-Aug-10     Release date:   13-Apr-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P06276  (CHLE_HUMAN) -  Cholinesterase
Seq:
Struc:
 
Seq:
Struc:
602 a.a.
531 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
+ 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   13 terms 
  Biochemical function     catalytic activity     9 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S1744309111004805 Acta Crystallogr Sect F Struct Biol Cryst Commun 67:434-437 (2011)
PubMed id: 21505234  
 
 
Cocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaine.
O.A.Asojo, O.A.Asojo, M.N.Ngamelue, K.Homma, O.Lockridge.
 
  ABSTRACT  
 
No abstract given.