1CER
DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION
Summary for 1CER
Entry DOI | 10.2210/pdb1cer/pdb |
Descriptor | HOLO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (2 entities in total) |
Functional Keywords | glycolysis, oxidoreductase, nad, oxidoreductase (aldehyde(d)-nad(a)) |
Biological source | Thermus aquaticus |
Cellular location | Cytoplasm: P00361 |
Total number of polymer chains | 8 |
Total formula weight | 292837.58 |
Authors | Tanner, J.J.,Hecht, R.M.,Krause, K.L. (deposition date: 1995-11-11, release date: 1996-03-08, Last modification date: 2024-02-07) |
Primary citation | Tanner, J.J.,Hecht, R.M.,Krause, K.L. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution. Biochemistry, 35:2597-2609, 1996 Cited by PubMed: 8611563DOI: 10.1021/bi951988q PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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