4WUO

Structure of the E270A Mutant Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH

Summary for 4WUO

Entry DOI	10.2210/pdb4wuo/pdb
Related	1HEX 2Y3Z 2Y40 2Y41 2Y42 4F7I
Descriptor	3-isopropylmalate dehydrogenase, 3-ISOPROPYLMALIC ACID, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (8 entities in total)
Functional Keywords	isopropylmalate dehydrogenase, ipmdh, oxidoreductase, mutant
Biological source	Thermus thermophilus
Cellular location	Cytoplasm: Q5SIY4
Total number of polymer chains	2
Total formula weight	79200.71
Authors	Pallo, A.,Graczer, E.,Olah, J.,Szimler, T.,Konarev, P.V.,Svergun, D.I.,Merli, A.,Zavodszky, P.,Vas, M.,Weiss, M.S. (deposition date: 2014-11-03, release date: 2014-11-12, Last modification date: 2024-01-10)
Primary citation	Graczer, E.,Pallo, A.,Olah, J.,Szimler, T.,Konarev, P.V.,Svergun, D.I.,Merli, A.,Zavodszky, P.,Weiss, M.S.,Vas, M. Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase. Febs Lett., 589:240-245, 2015 Cited by PubMed: 25497013 DOI: 10.1016/j.febslet.2014.12.005 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.05 Å)

Structure validation