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3EI5

Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with PLP-Glu: an external aldimine mimic

Summary for 3EI5
Entry DOI10.2210/pdb3ei5/pdb
Related3EI6 3EI7 3EI8 3EI9 3EIA 3EIB
DescriptorLL-diaminopimelate aminotransferase, N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid, GLYCEROL, ... (5 entities in total)
Functional Keywordsaminotransferase, lysine biosynthesis, pyridoxal 5' phosphate, external aldimine, ll-diaminopimelate, chloroplast, pyridoxal phosphate, transferase, transit peptide
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
Cellular locationPlastid, chloroplast: Q93ZN9
Total number of polymer chains2
Total formula weight96352.34
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 citationWatanabe, 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: 18952095
DOI: 10.1016/j.jmb.2008.10.022
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

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