1PSD
THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE
Summary for 1PSD
| Entry DOI | 10.2210/pdb1psd/pdb |
| Descriptor | D-3-PHOSPHOGLYCERATE DEHYDROGENASE (PHOSPHOGLYCERATE DEHYDROGENASE), NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SERINE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase (nad(a)) |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 89727.90 |
| Authors | Schuller, D.J.,Grant, G.A.,Banaszak, L.J. (deposition date: 1995-05-02, release date: 1995-07-31, Last modification date: 2024-02-14) |
| Primary citation | Schuller, D.J.,Grant, G.A.,Banaszak, L.J. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat.Struct.Biol., 2:69-76, 1995 Cited by PubMed Abstract: The crystal structure of the phosphoglycerate dehydrogenase from Escherichia coli is unique among dehydrogenases. It consists of three clearly separate domains connected by flexible hinges. The tetramer has approximate 222 symmetry with the principal contacts between the subunits forming between either the nucleotide binding domains or the regulatory domains. Two slightly different subunit conformations are present which vary only in the orientations of the domains. There is a hinge-like arrangement near the active site cleft and the serine effector site is provided by the regulatory domain of each of two subunits. Interdomain flexibility may play a key role in both catalysis and allosteric inhibition. PubMed: 7719856DOI: 10.1038/nsb0195-69 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
Download full validation report
