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2VK1

Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant D28A in complex with its substrate

Summary for 2VK1
Entry DOI10.2210/pdb2vk1/pdb
Related1PVD 1PYD 1QPB
DescriptorPYRUVATE DECARBOXYLASE ISOZYME 1, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsasymmetric 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 sourceSACCHAROMYCES CEREVISIAE (YEAST)
Total number of polymer chains4
Total formula weight248554.96
Authors
Kutter, S.,Weik, M.,Weiss, M.S.,Konig, S. (deposition date: 2007-12-16, release date: 2009-01-27, Last modification date: 2023-12-13)
Primary citationKutter, 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 (1.71 Å)
Structure validation

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