1LTH

T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL

Summary for 1LTH

Entry DOI	10.2210/pdb1lth/pdb
Descriptor	L-LACTATE DEHYDROGENASE (T- AND R- STATE TETRAMER COMPLEX), 1,6-di-O-phosphono-beta-D-fructofuranose, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
Functional Keywords	oxidoreductase, choh(d)-nad(a), allosteric enzyme
Biological source	Bifidobacterium longum subsp. longum
Cellular location	Cytoplasm: P19869
Total number of polymer chains	2
Total formula weight	70353.69
Authors	Iwata, S.,Ohta, T. (deposition date: 1995-01-04, release date: 1995-03-31, Last modification date: 2024-02-14)
Primary citation	Iwata, S.,Kamata, K.,Yoshida, S.,Minowa, T.,Ohta, T. T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control. Nat.Struct.Biol., 1:176-185, 1994 Cited by PubMed: 7656036 DOI: 10.1038/nsb0394-176 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation