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; PubMed: 8611563; DOI: 10.1021/bi951988q

Experimental method

X-RAY DIFFRACTION (2.5 Å)