3L76
Crystal Structure of Aspartate Kinase from Synechocystis
Summary for 3L76
Entry DOI | 10.2210/pdb3l76/pdb |
Descriptor | Aspartokinase, THREONINE, LYSINE, ... (5 entities in total) |
Functional Keywords | aspartokinase, synechocystis, allostery, act domains, kinase, transferase |
Biological source | Synechocystis |
Total number of polymer chains | 2 |
Total formula weight | 128357.06 |
Authors | Robin, A.,Cobessi, D.,Curien, G.,Robert-Genthon, M.,Ferrer, J.-L.,Dumas, R. (deposition date: 2009-12-28, release date: 2010-06-09, Last modification date: 2024-03-20) |
Primary citation | Robin, A.Y.,Cobessi, D.,Curien, G.,Robert-Genthon, M.,Ferrer, J.-L.,Dumas, R. A new mode of dimerization of allosteric enzymes with ACT domains revealed by the crystal structure of the aspartate kinase from Cyanobacteria J.Mol.Biol., 399:283-293, 2010 Cited by PubMed: 20398676DOI: 10.1016/j.jmb.2010.04.014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.54 Å) |
Structure validation
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