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: 2011-07-13)
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: 16731588 DOI: 10.1105/TPC.105.040451 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.85 Å)

Structure validation