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TitleTwo crystal structures of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveal protein-ligand interactions including a structural basis for observed antifolate resistance.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 61, Page 258-262, Year 2005
Publish dateFeb 17, 2004 (structure data deposition date)
AuthorsAnderson, A.C.
External linksActa Crystallogr. ,Sect. F / PubMed:16511011
MethodsX-ray diffraction
Resolution2.87 Å
Structure data

PDB-1sej:
Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP
Method: X-RAY DIFFRACTION / Resolution: 2.87 Å

Chemicals

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

ChemComp-F89:
S)-2-(5(((1,2-DIHYDRO-3-METHYL-1-OXOBENZO(F)QUINAZOLIN-9-YL)METHYL)AMINO)1-OXO-2-ISOINDOLINYL)GLUTARIC ACID

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-HOH:
WATER

Source
  • cryptosporidium hominis (eukaryote)
KeywordsTRANSFERASE / OXIDOREDUCTASE / bifunctional enzyme

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