1HEX

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

Summary for 1HEX

• Entry DOI: 10.2210/pdb1hex/pdb
• Descriptor: 3-ISOPROPYLMALATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: Q5SIY4
• Total number of polymer chains: 1
• Total formula weight: 37488.59

Authors

Hurley, J.H. (deposition date: 1994-09-09, release date: 1994-12-20, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)