2VJY
Pyruvate decarboxylase from Kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate
Summary for 2VJY
| Entry DOI | 10.2210/pdb2vjy/pdb |
| Related | 2G1I 2VK4 |
| Descriptor | PYRUVATE DECARBOXYLASE, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | metal-binding, decarboxylase, dimer of dimers, methylacetylphosphonate, methyl acetylphosphonate, substrate activation, thiamine diphosphate, thiamine pyrophosphate, asymmetric active sites, map, lyase, pyruvate, magnesium, flavoprotein |
| Biological source | KLUYVEROMYCES LACTIS (YEAST) |
| Total number of polymer chains | 4 |
| Total formula weight | 250200.30 |
| Authors | Kutter, S.,Wille, G.,Weiss, M.S.,Konig, S. (deposition date: 2007-12-14, 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 (2.3 Å) |
Structure validation
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