3EIA

Crystal structure of K270Q variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with L-Glu: External aldimine form

3EIA の概要

• エントリーDOI: 10.2210/pdb3eia/pdb
• 関連するPDBエントリー: 3EI5 3EI6 3EI7 3EI8 3EI9 3EIB
• 分子名称: LL-diaminopimelate aminotransferase, SULFATE ION, (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid, ... (4 entities in total)
• 機能のキーワード: aminotransferase, lysine biosynthesis, pyridoxal 5' phosphate, external aldimine, ll-diaminopimelate, chloroplast, plastid, pyridoxal phosphate, transferase, transit peptide
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Plastid, chloroplast: Q93ZN9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95977.83

構造登録者

Watanabe, N.,Clay, M.D.,van Belkum, M.J.,Cherney, M.M.,Vederas, J.C.,James, M.N.G. (登録日: 2008-09-15, 公開日: 2008-10-14, 最終更新日: 2023-08-30)

• 主引用文献: 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; PubMed: 18952095; DOI: 10.1016/j.jmb.2008.10.022

実験手法

X-RAY DIFFRACTION (1.85 Å)