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TitleAlanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptides.
Journal, issue, pagesJ. Med. Chem., Vol. 58, Page 1012-1018, Year 2015
Publish dateJun 4, 2012 (structure data deposition date)
AuthorsTochowicz, A. / Santucci, M. / Saxena, P. / Guaitoli, G. / Trande, M. / Finer-Moore, J. / Stroud, R.M. / Costi, M.P.
External linksJ. Med. Chem. / PubMed:25427005
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-4fgt:
Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes inactive conformation of the enzyme.
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic (others)
Keywordstransferase/transferase inhibitor / dimer / mutant K47A of hTS / inactive hTS conformation / hTS complex with peptidic inhibitor / transferase-transferase inhibitor complex

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