1GAD
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Summary for 1GAD
Entry DOI | 10.2210/pdb1gad/pdb |
Descriptor | D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
Functional Keywords | oxidoreductase (aldehyde(d)-nad+(a)) |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A9B2 |
Total number of polymer chains | 2 |
Total formula weight | 72219.33 |
Authors | Duee, E.,Olivier-Deyris, L.,Fanchon, E.,Corbier, C.,Branlant, G.,Dideberg, O. (deposition date: 1995-10-24, release date: 1996-03-08, Last modification date: 2024-02-07) |
Primary citation | Duee, E.,Olivier-Deyris, L.,Fanchon, E.,Corbier, C.,Branlant, G.,Dideberg, O. Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity. J.Mol.Biol., 257:814-838, 1996 Cited by PubMed: 8636984DOI: 10.1006/jmbi.1996.0204 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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