1HEX

STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE IN COMPLEX WITH NAD+: LIGAND-INDUCED LOOP-CLOSING AND MECHANISM FOR COFACTOR SPECIFICITY

1HEX の概要

• エントリーDOI: 10.2210/pdb1hex/pdb
• 分子名称: 3-ISOPROPYLMALATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm: Q5SIY4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37488.59

構造登録者

Hurley, J.H. (登録日: 1994-09-09, 公開日: 1994-12-20, 最終更新日: 2024-02-07)

主引用文献

Hurley, J.H.,Dean, A.M.
Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity.
Structure, 2:1007-1016, 1994

PubMed Abstract: The leucine biosynthetic enzyme 3-isopropylmalate dehydrogenase (IMDH) belongs to a unique class of bifunctional decarboxylating dehydrogenases. The two best-known members of this family, IMDH and isocitrate dehydrogenase (IDH), share a common structural framework and catalytic mechanism but have different substrate and cofactor specificities. IMDH is NAD(+)-dependent, while IDHs occur in both NAD(+)-dependent and NADP(+)-dependent forms.

PubMed: 7881901
DOI: 10.1016/S0969-2126(94)00104-9

実験手法

X-RAY DIFFRACTION (2.5 Å)