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PDBsum entry 2cje

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protein ligands metals links
Hydrolase PDB id
2cje
Jmol
Contents
Protein chain
258 a.a. *
Ligands
DUN
Metals
_MG ×3
Waters ×88
* Residue conservation analysis
PDB id:
2cje
Name: Hydrolase
Title: The crystal structure of a complex of leishmania major dutpase with substrate analogue dupnhp
Structure: Dutpase. Chain: a. Synonym: deoxyuridine triphosphatase, dutp diphosphatase, d pyrophosphatase. Engineered: yes
Source: Leishmania major. Organism_taxid: 5664. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.34Å     R-factor:   0.187     R-free:   0.238
Authors: O.V.Moroz,M.J.Fogg,D.Gonzalez-Pacanowska,K.S.Wilson
Key ref: G.R.Hemsworth et al. (2011). The crystal structure of the Leishmania major deoxyuridine triphosphate nucleotidohydrolase in complex with nucleotide analogues, dUMP, and deoxyuridine. J Biol Chem, 286, 16470-16481. PubMed id: 21454646 DOI: 10.1074/jbc.M111.224873
Date:
31-Mar-06     Release date:   17-Apr-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O15826  (O15826_LEIMA) -  DUTPase
Seq:
Struc:
268 a.a.
258 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.6.1.23  - dUTP diphosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: dUTP + H2O = dUMP + diphosphate
dUTP
+ H(2)O
=
dUMP
Bound ligand (Het Group name = DUN)
matches with 76.00% similarity
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     hydrolase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M111.224873 J Biol Chem 286:16470-16481 (2011)
PubMed id: 21454646  
 
 
The crystal structure of the Leishmania major deoxyuridine triphosphate nucleotidohydrolase in complex with nucleotide analogues, dUMP, and deoxyuridine.
G.R.Hemsworth, O.V.Moroz, M.J.Fogg, B.Scott, C.Bosch-Navarrete, D.González-Pacanowska, K.S.Wilson.
 
  ABSTRACT  
 
No abstract given.