3C3U

Crystal structure of AKR1C1 in complex with NADP and 3,5-dichlorosalicylic acid

3C3U の概要

• エントリーDOI: 10.2210/pdb3c3u/pdb
• 分子名称: Aldo-keto reductase family 1 member C1, ZINC ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: aldo-keto reductase, 20 alpha hydroxysteroid dehydrogenase, akr1c1, cytoplasm, nadp, oxidoreductase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: Q04828
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37855.16

構造登録者

Dhagat, U.,El-Kabbani, O. (登録日: 2008-01-28, 公開日: 2008-08-26, 最終更新日: 2023-11-01)

主引用文献

Dhagat, U.,Endo, S.,Sumii, R.,Hara, A.,El-Kabbani, O.
Selectivity determinants of inhibitor binding to human 20alpha-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid
J.Med.Chem., 51:4844-4848, 2008

PubMed Abstract: The crystal structure of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) in ternary complex with the coenzyme NADP (+) and the potent inhibitor 3,5-dichlorosalicylic acid was determined at a resolution of 1.8 A. The inhibitor is held in place by a network of hydrogen bonding interactions with the active site residues Tyr55, His117, and His222. The important role of the nonconserved residues Leu54, His222, Leu306, and Leu308 in inhibitor binding and selectivity was determined by site-directed mutagenesis.

PubMed: 18620380
DOI: 10.1021/jm8003575

実験手法

X-RAY DIFFRACTION (1.8 Å)