spacer
spacer

PDBsum entry 2xqf

Go to PDB code: 
protein ligands metals links
Hydrolase PDB id
2xqf
Jmol
Contents
Protein chain
527 a.a.
Ligands
GLY
UNX ×18
UNX-UNX-UNX ×4
UNX-UNX ×3
_VX
SO4 ×2
NAG-NAG-FUL ×2
NAG ×4
Metals
_NA
_CL ×2
__K
Waters ×432
PDB id:
2xqf
Name: Hydrolase
Title: X-ray structure of human butyrylcholinesterase inhibited by vx
Structure: Cholinesterase. Chain: a. Fragment: residues 31-557. Synonym: acylcholine acylhydrolase, choline esterase ii, butyrylcholine esterase, pseudocholinesterase. 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:
2.10Å     R-factor:   0.150     R-free:   0.189
Authors: M.Wandhammer,E.Carletti,E.Gillon,P.Masson,M.Goeldner,D.Noort
Key ref: M.Wandhammer et al. (2011). Structural study of the complex stereoselectivity of human butyrylcholinesterase for the neurotoxic V-agents. J Biol Chem, 286, 16783-16789. PubMed id: 21454498
Date:
02-Sep-10     Release date:   23-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06276  (CHLE_HUMAN) -  Cholinesterase
Seq:
Struc:
 
Seq:
Struc:
602 a.a.
528 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 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
Bound ligand (Het Group name = GLY)
matches with 50.00% similarity
+ 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    
 
 
J Biol Chem 286:16783-16789 (2011)
PubMed id: 21454498  
 
 
Structural study of the complex stereoselectivity of human butyrylcholinesterase for the neurotoxic V-agents.
M.Wandhammer, E.Carletti, M.Van der Schans, E.Gillon, Y.Nicolet, P.Masson, M.Goeldner, D.Noort, F.Nachon.
 
  ABSTRACT  
 
No abstract given.