3EI9
Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with L-Glu: External aldimine form
Summary for 3EI9
Entry DOI | 10.2210/pdb3ei9/pdb |
Related | 3EI5 3EI6 3EI7 3EI8 3EIA 3EIB |
Descriptor | LL-diaminopimelate aminotransferase, (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid, GLYCEROL, ... (5 entities in total) |
Functional Keywords | aminotransferase, lysine biosynthesis, pyridoxal 5' phosphate, external aldimine, ll-diaminopimelate, chloroplast, pyridoxal phosphate, transferase, transit peptide |
Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
Cellular location | Plastid, chloroplast: Q93ZN9 |
Total number of polymer chains | 2 |
Total formula weight | 96598.40 |
Authors | Watanabe, N.,Clay, M.D.,van Belkum, M.J.,Cherney, M.M.,Vederas, J.C.,James, M.N.G. (deposition date: 2008-09-15, release date: 2008-10-14, Last modification date: 2023-08-30) |
Primary citation | Watanabe, N.,Clay, M.D.,van Belkum, M.J.,Cherney, M.M.,Vederas, J.C.,James, M.N. Mechanism of substrate recognition and PLP-induced conformational changes in LL-diaminopimelate aminotransferase from Arabidopsis thaliana. J.Mol.Biol., 384:1314-1329, 2008 Cited by PubMed: 18952095DOI: 10.1016/j.jmb.2008.10.022 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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