2CDQ
Crystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionine
Summary for 2CDQ
Entry DOI | 10.2210/pdb2cdq/pdb |
Descriptor | ASPARTOKINASE, LYSINE, D(-)-TARTARIC ACID, ... (5 entities in total) |
Functional Keywords | aspartate kinase, amino acid metabolism, act domain, allostery, s-adenosylmethionine, lysine, allosteric effector, plant, transferase, amino acid biosynthesis |
Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
Cellular location | Plastid, chloroplast (Potential): Q9LYU8 |
Total number of polymer chains | 2 |
Total formula weight | 113606.51 |
Authors | Mas-Droux, C.,Curien, G.,Robert-Genthon, M.,Laurencin, M.,Ferrer, J.L.,Dumas, R. (deposition date: 2006-01-26, release date: 2006-05-30, Last modification date: 2024-05-08) |
Primary citation | Mas-Droux, C.,Curien, G.,Robert-Genthon, M.,Laurencin, M.,Ferrer, J.L.,Dumas, R. A Novel Organization of Act Domains in Allosteric Enzymes Revealed by the Crystal Structure of Arabidopsis Aspartate Kinase Plant Cell, 18:1681-, 2006 Cited by PubMed: 16731588DOI: 10.1105/TPC.105.040451 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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