1PGQ

CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM

Summary for 1PGQ

Entry DOI	10.2210/pdb1pgq/pdb
Related	1PGN 1PGO 1PGP 2PGD
Descriptor	6-PHOSPHOGLUCONATE DEHYDROGENASE, SULFATE ION, ADENOSINE-2'-MONOPHOSPHATE, ... (4 entities in total)
Functional Keywords	oxidoreductase (choh(d)-nadp+(a))
Biological source	Ovis aries (sheep)
Cellular location	Cytoplasm : P00349
Total number of polymer chains	1
Total formula weight	53541.06
Authors	Adams, M.J.,Phillips, C.,Gover, S. (deposition date: 1994-07-18, release date: 1995-02-27, Last modification date: 2024-02-14)
Primary citation	Adams, M.J.,Ellis, G.H.,Gover, S.,Naylor, C.E.,Phillips, C. Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism. Structure, 2:651-668, 1994 Cited by PubMed Abstract: The nicotinamide adenine dinucleotide phosphate (NADP)-dependent oxidative decarboxylase, 6-phosphogluconate dehydrogenase, is a major source of reduced coenzyme for synthesis. Enzymes later in the pentose phosphate pathway convert the reaction product, ribulose 5-phosphate, to ribose 5-phosphate. Crystallographic study of complexes with coenzyme and substrate explain the NADP dependence which determines the enzyme's metabolic role and support the proposed general base-general acid mechanism. PubMed: 7922042 DOI: 10.1016/S0969-2126(00)00066-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.17 Å)

Structure validation