2VK8

Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate

Summary for 2VK8

Entry DOI	10.2210/pdb2vk8/pdb
Related	1PVD 1PYD 1QPB 2VK1
Descriptor	PYRUVATE DECARBOXYLASE ISOZYME 1, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	asymmetric active sites, phenylalanine catabolism, tryptophan catabolism, thiamine pyrophosphate, dimer of dimers, phosphorylation, allosteric enzyme, tdp, tpp, lyase, nucleus, pyruvate, cytoplasm, branched-chain amino acid catabolism, substrate activation, thiamine diphosphate, magnesium, acetylation, metal-binding, decarboxylase
Biological source	SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
Total number of polymer chains	4
Total formula weight	248502.96
Authors	Kutter, S.,Weik, M.,Weiss, M.S.,Konig, S. (deposition date: 2007-12-17, release date: 2009-01-27, Last modification date: 2023-12-13)
Primary citation	Kutter, S.,Weiss, M.S.,Wille, G.,Golbik, R.,Spinka, M.,Konig, S. Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation. J.Biol.Chem., 284:12136-, 2009 Cited by PubMed: 19246454 DOI: 10.1074/JBC.M806228200 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.42 Å)

Structure validation