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6IDJ

Crystal structure of human DHODH in complex with ferulenol

6IDJ の概要
エントリーDOI10.2210/pdb6idj/pdb
分子名称Dihydroorotate dehydrogenase (quinone), mitochondrial, SULFATE ION, ACETATE ION, ... (7 entities in total)
機能のキーワードcoccidium, mitochondria, electron transport chain, dihydroorotate dehydrogenase, membrane protein
由来する生物種Homo sapiens (Human)
タンパク質・核酸の鎖数1
化学式量合計44080.67
構造登録者
主引用文献Sato, D.,Hartuti, E.D.,Inaoka, D.K.,Sakura, T.,Amalia, E.,Nagahama, M.,Yoshioka, Y.,Tsuji, N.,Nozaki, T.,Kita, K.,Harada, S.,Matsubayashi, M.,Shiba, T.
Structural and Biochemical Features of Eimeria tenella Dihydroorotate Dehydrogenase, a Potential Drug Target.
Genes (Basel), 11:-, 2020
Cited by
PubMed Abstract: Dihydroorotate dehydrogenase (DHODH) is a mitochondrial monotopic membrane protein that plays an essential role in the pyrimidine de novo biosynthesis and electron transport chain pathways. In , an intracellular apicomplexan parasite that causes the most severe form of chicken coccidiosis, the activity of pyrimidine salvage pathway at the intracellular stage is negligible and it relies on the pyrimidine de novo biosynthesis pathway. Therefore, the enzymes of the de novo pathway are considered potential drug target candidates for the design of compounds with activity against this parasite. Although, DHODHs from (EtDHODH), (PfDHODH), and human (HsDHODH) show distinct sensitivities to classical DHODH inhibitors, in this paper, we identify ferulenol as a potent inhibitor of both EtDHODH and HsDHODH. Additionally, we report the crystal structures of EtDHODH and HsDHODH in the absence and presence of ferulenol. Comparison of these enzymes showed that despite similar overall structures, the EtDHODH has a long insertion in the N-terminal helix region that assumes a disordered configuration. In addition, the crystal structures revealed that the ferulenol binding pocket of EtDHODH is larger than that of HsDHODH. These differences can be explored to accelerate structure-based design of inhibitors specifically targeting EtDHODH.
PubMed: 33297567
DOI: 10.3390/genes11121468
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 6idj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-09に公開中

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