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: 19246454DOI: 10.1074/JBC.M806228200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.42 Å) |
Structure validation
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