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Structure paper

TitleAn alternative conformation of the N-terminal loop of human dihydroorotate dehydrogenase drives binding to a potent antiproliferative agent.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 80, Page 386-396, Year 2024
Publish dateDec 1, 2023 (structure data deposition date)
AuthorsAlberti, M. / Poli, G. / Broggini, L. / Sainas, S. / Rizzi, M. / Boschi, D. / Ferraris, D.M. / Martino, E. / Ricagno, S. / Tuccinardi, T. ...Alberti, M. / Poli, G. / Broggini, L. / Sainas, S. / Rizzi, M. / Boschi, D. / Ferraris, D.M. / Martino, E. / Ricagno, S. / Tuccinardi, T. / Lolli, M.L. / Miggiano, R.
External linksActa Crystallogr D Struct Biol / PubMed:38805244
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-8rak:
Crystal structure of human Dihydroorotate Dehydrogenase in complex with the inhibitor 2-Hydroxy-N-(2-isopropyl-5-methyl-4-(pyridin-4-yloxy)phenyl)pyrazolo[1,5-a]pyridine-3-carboxamide
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-ORO:
OROTIC ACID


ChemComp, No image

ChemComp-YMH:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsFLAVOPROTEIN / Drug discovery / DHODH / inhibitor / leukemia / protein binding

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