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Structure paper

TitleStructures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 3051-3059, Year 2005
Publish dateOct 18, 2004 (structure data deposition date)
AuthorsJohansson, E. / Fano, M. / Bynck, J.H. / Neuhard, J. / Larsen, S. / Sigurskjold, B.W. / Christensen, U. / Willemoes, M.
External linksJ. Biol. Chem. / PubMed:15539408
MethodsX-ray diffraction
Resolution1.8 - 2.53 Å
Structure data

PDB-1xs1:
dCTP deaminase from Escherichia coli in complex with dUTP
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1xs4:
dCTP deaminase from Escherichia coli- E138A mutant enzyme in complex with dCTP
Method: X-RAY DIFFRACTION / Resolution: 2.53 Å

PDB-1xs6:
dCTP deaminase from Escherichia coli. E138A mutant enzyme in complex with dUTP
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-DUT:
DEOXYURIDINE-5'-TRIPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-DCP:
2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / dCTP deaminase / nucleotide metabolism / trimer

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