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TitleThe only active mutant of thymidylate synthase D169, a residue far from the site of methyl transfer, demonstrates the exquisite nature of enzyme specificity.
Journal, issue, pagesProtein Eng., Vol. 16, Page 229-240, Year 2003
Publish dateDec 5, 2002 (structure data deposition date)
AuthorsBirdsall, D.L. / Finer-Moore, J. / Stroud, R.M.
External linksProtein Eng. / PubMed:12702803
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-1nce:
Crystal structure of a ternary complex of E. coli thymidylate synthase D169C with dUMP and the antifolate CB3717
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-UMP:
2'-DEOXYURIDINE 5'-MONOPHOSPHATE

ChemComp-CB3:
10-PROPARGYL-5,8-DIDEAZAFOLIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • escherichia coli o157:h7 (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / beta-sheet interface / protein-dUMP-cofactor analog complex / asymmetric dimer

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