1psd | pdb_00001psd
THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE
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Overview
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.
About this Structure
1PSD is a Single protein structure of sequence from Escherichia coli k12 with NAD and SER as ligands. Active as Phosphoglycerate dehydrogenase, with EC number 1.1.1.95 Full crystallographic information is available from OCA.
Reference
The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase., Schuller DJ, Grant GA, Banaszak LJ, Nat Struct Biol. 1995 Jan;2(1):69-76. PMID:7719856
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