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PDBsum entry 3kgg

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protein metals links
Hydrolase PDB id
3kgg
Jmol
Contents
Protein chain
313 a.a. *
Metals
_CA ×2
Waters ×189
* Residue conservation analysis
PDB id:
3kgg
Name: Hydrolase
Title: X-ray structure of perdeuterated diisopropyl fluorophosphata (dfpase): perdeuteration of proteins for neutron diffractio
Structure: Diisopropyl-fluorophosphatase. Chain: a. Synonym: dfpase. Engineered: yes
Source: Loligo vulgaris. Common european squid. Organism_taxid: 6622. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.10Å     R-factor:   0.176     R-free:   0.217
Authors: M.-M.Blum,S.J.Tomanicek,H.John,B.L.Hanson,H.R.Terjans,B.P.Sc P.Langan,J.C.-H.Chen
Key ref: M.M.Blum et al. (2010). X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 379-385. PubMed id: 20383004
Date:
29-Oct-09     Release date:   07-Apr-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q7SIG4  (DFPA_LOLVU) -  Diisopropyl-fluorophosphatase
Seq:
Struc:
314 a.a.
313 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.8.2  - Diisopropyl-fluorophosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
Diisopropyl fluorophosphate
+ H(2)O
= diisopropyl phosphate
+ fluoride
      Cofactor: Divalent cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biological_process   2 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
    Added reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 66:379-385 (2010)
PubMed id: 20383004  
 
 
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction.
M.M.Blum, S.J.Tomanicek, H.John, B.L.Hanson, H.Rüterjans, B.P.Schoenborn, P.Langan, J.C.Chen.
 
  ABSTRACT  
 
The signal-to-noise ratio is one of the limiting factors in neutron macromolecular crystallography. Protein perdeuteration, which replaces all H atoms with deuterium, is a method of improving the signal-to-noise ratio of neutron crystallography experiments by reducing the incoherent scattering of the hydrogen isotope. Detailed analyses of perdeuterated and hydrogenated structures are necessary in order to evaluate the utility of perdeuterated crystals for neutron diffraction studies. The room-temperature X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase) is reported at 2.1 A resolution. Comparison with an independently refined hydrogenated room-temperature structure of DFPase revealed no major systematic differences, although the crystals of perdeuterated DFPase did not diffract neutrons. The lack of diffraction is examined with respect to data-collection and crystallographic parameters. The diffraction characteristics of successful neutron structure determinations are presented as a guideline for future neutron diffraction studies of macromolecules. X-ray diffraction to beyond 2.0 A resolution appears to be a strong predictor of successful neutron structures.