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 | |
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: 7656036DOI: 10.1038/nsb0394-176 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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