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1A5Z

LACTATE DEHYDROGENASE FROM THERMOTOGA MARITIMA (TMLDH)

Summary for 1A5Z
Entry DOI10.2210/pdb1a5z/pdb
DescriptorL-LACTATE DEHYDROGENASE, 1,6-di-O-phosphono-beta-D-fructofuranose, CADMIUM ION, ... (6 entities in total)
Functional Keywordsoxidoreductase, glycolysis, hyperthermophiles, thermotoga maritima, protein stability
Biological sourceThermotoga maritima
Cellular locationCytoplasm: P16115
Total number of polymer chains1
Total formula weight36796.33
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 citationAuerbach, 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: 9655830
DOI: 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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