4D9M
Crystal structure of Diaminopropionate ammonia lyase from Escherichia coli in complex with aminoacrylate-PLP azomethine reaction intermediate
Summary for 4D9M
Entry DOI | 10.2210/pdb4d9m/pdb |
Related | 4D9G 4D9I 4D9K 4D9N |
Descriptor | Diaminopropionate ammonia-lyase, 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid (3 entities in total) |
Functional Keywords | fold type ii plp-dependent enzyme, tryptophan synthase beta subunit-like plp-dependent enzymes superfamily, lyase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 87377.24 |
Authors | Bisht, S.,Rajaram, V.,Bharath, S.R.,Murthy, M.R.N. (deposition date: 2012-01-11, release date: 2012-04-25, Last modification date: 2023-11-08) |
Primary citation | Bisht, S.,Rajaram, V.,Bharath, S.R.,Kalyani, J.N.,Khan, F.,Rao, A.N.,Savithri, H.S.,Murthy, M.R.N. Crystal Structure of Escherichia coli Diaminopropionate Ammonia-lyase Reveals Mechanism of Enzyme Activation and Catalysis J.Biol.Chem., 287:20369-20381, 2012 Cited by PubMed: 22505717DOI: 10.1074/jbc.M112.351809 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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