1A5Z
LACTATE DEHYDROGENASE FROM THERMOTOGA MARITIMA (TMLDH)
Summary for 1A5Z
Entry DOI | 10.2210/pdb1a5z/pdb |
Descriptor | L-LACTATE DEHYDROGENASE, 1,6-di-O-phosphono-beta-D-fructofuranose, CADMIUM ION, ... (6 entities in total) |
Functional Keywords | oxidoreductase, glycolysis, hyperthermophiles, thermotoga maritima, protein stability |
Biological source | Thermotoga maritima |
Cellular location | Cytoplasm: P16115 |
Total number of polymer chains | 1 |
Total formula weight | 36796.33 |
Authors | Auerbach, G.,Ostendorp, R.,Prade, L.,Korndoerfer, I.,Dams, T.,Huber, R.,Jaenicke, R. (deposition date: 1998-02-18, release date: 1999-03-23, Last modification date: 2020-07-29) |
Primary citation | Auerbach, G.,Ostendorp, R.,Prade, L.,Korndorfer, I.,Dams, T.,Huber, R.,Jaenicke, R. Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization. Structure, 6:769-781, 1998 Cited by PubMed: 9655830DOI: 10.1016/S0969-2126(98)00078-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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