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Structure paper

TitleStructure-activity relationships of orotidine-5'-monophosphate decarboxylase inhibitors as anticancer agents.
Journal, issue, pagesJ. Med. Chem., Vol. 52, Page 1648-1658, Year 2009
Publish dateFeb 2, 2009 (structure data deposition date)
AuthorsBello, A.M. / Konforte, D. / Poduch, E. / Furlonger, C. / Wei, L. / Liu, Y. / Lewis, M. / Pai, E.F. / Paige, C.J. / Kotra, L.P.
External linksJ. Med. Chem. / PubMed:19260677
MethodsX-ray diffraction
Resolution1.4 - 1.7 Å
Structure data

PDB-3g3d:
Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-azido-UMP
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3g3m:
Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-iodo-UMP
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-3s9y:
Crystal Structure of P. falciparum orotidine 5'-monophosphate decarboxylase complexed with 5-fluoro-6-amino-UMP in space group P21, produced from 5-fluoro-6-azido-UMP
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-5FU:
5-FLUORO-URIDINE-5'-MONOPHOSPHATE

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-FNU:
6-amino-5-fluorouridine 5'-(dihydrogen phosphate)

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

Source
  • homo sapiens (human)
  • plasmodium falciparum (malaria parasite P. falciparum)
KeywordsLYASE / UMP synthase / c-terminal Domain / Orotidine 5'-monophosphate Decarboxylase / human / 5-fluoro-6-azido-UMP / Decarboxylase / Disease mutation / Glycosyltransferase / Multifunctional enzyme / Phosphoprotein / Pyrimidine biosynthesis / Transferase / 5-fluoro-6-iodo-UMP / Alternative splicing / Polymorphism / P. falciparum / 5-fluoro-6-amino-UMP

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