4AON
Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex
Summary for 4AON
Entry DOI | 10.2210/pdb4aon/pdb |
Related | 1AW8 1PPY 1PQE 1PQF 1PQH 1PT0 1PT1 1PYQ 1PYU 4AOK |
Descriptor | ASPARTATE-ALPHA-DECARBOXYLASE BETA CHAIN, ASPARTATE-ALPHA-DECARBOXYLASE ALPHA CHAIN, GLUTAMIC ACID, ... (4 entities in total) |
Functional Keywords | hydrolase, amino acid metabolism, protein-derived cofactor. |
Biological source | ESCHERICHIA COLI More |
Cellular location | Cytoplasm: P0A790 P0A790 |
Total number of polymer chains | 4 |
Total formula weight | 31856.01 |
Authors | Yorke, B.A.,Monteiro, D.C.F.,Pearson, A.R.,Webb, M.E. (deposition date: 2012-03-29, release date: 2012-10-31, Last modification date: 2023-12-20) |
Primary citation | Yorke, B.A.,Monteiro, D.C.F.,Pearson, A.R.,Webb, M.E. Conformational Dynamics of Aspartate Alpha Decarboxylase Active Site Revealed by Protein-Ligand Complexes To be Published, |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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