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2Z1Z

Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana complexed with L-malate ion

Summary for 2Z1Z
Entry DOI10.2210/pdb2z1z/pdb
DescriptorLL-diaminopimelate aminotransferase, D-MALATE, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
Functional Keywordsll-diaminopimelate aminotransferase, ll-dap-at, plp, arabidopsis thaliana, lysine biosynthesis, thdpa, ll-dap, transferase
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains2
Total formula weight95663.67
Authors
Watanabe, N.,Cherney, M.M.,van Belkum, M.J.,Marcus, S.L.,Flegel, M.D.,Clay, M.D.,Deyholos, M.K.,Vederas, J.C.,James, M.N.G. (deposition date: 2007-05-16, release date: 2007-07-17, Last modification date: 2024-04-03)
Primary citationWatanabe, N.,Cherney, M.M.,van Belkum, M.J.,Marcus, S.L.,Flegel, M.D.,Clay, M.D.,Deyholos, M.K.,Vederas, J.C.,James, M.N.
Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia
J.Mol.Biol., 371:685-702, 2007
Cited by
PubMed: 17583737
DOI: 10.1016/j.jmb.2007.05.061
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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