6J3C

Crystal structure of human DHODH in complex with inhibitor 1291

Summary for 6J3C

• Entry DOI: 10.2210/pdb6j3c/pdb
• Descriptor: Dihydroorotate dehydrogenase (quinone), mitochondrial, SULFATE ION, FLAVIN MONONUCLEOTIDE, ... (7 entities in total)
• Functional Keywords: dhodh, inhibitor, complex, oxidoreductase, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 41361.90

Authors

Yu, Y.,Chen, Q. (deposition date: 2019-01-04, release date: 2019-08-21, Last modification date: 2024-03-27)

Primary citation

Zeng, T.,Zuo, Z.,Luo, Y.,Zhao, Y.,Yu, Y.,Chen, Q.
A novel series of human dihydroorotate dehydrogenase inhibitors discovered by in vitro screening: inhibition activity and crystallographic binding mode.
Febs Open Bio, 9:1348-1354, 2019

PubMed Abstract: Human dihydroorotate dehydrogenase (DHODH), the enzyme that catalyzes the rate-limiting step in de novo pyrimidine biosynthesis, is considered to be an attractive target for potential treatment of autoimmune disease and cancer. Here, we present a novel class of human DHODH inhibitors with high inhibitory potency. The high-resolution crystal structures of human DHODH complexed with various agents reveal the details of their interactions. Comparisons with the binding modes of teriflunomide and brequinar provide insights that may facilitate the development of new inhibitors targeting human DHODH.

PubMed: 31087527
DOI: 10.1002/2211-5463.12658

Experimental method

X-RAY DIFFRACTION (1.851 Å)