1PQH
Serine 25 to Threonine mutation of aspartate decarboxylase
Summary for 1PQH
Entry DOI | 10.2210/pdb1pqh/pdb |
Related | 1aw8 1PPY 1PQE 1PQF 1PT0 1PT1 1PYQ 1PYU |
Descriptor | Aspartate 1-decarboxylase, SODIUM ION, MALONIC ACID, ... (4 entities in total) |
Functional Keywords | pyruvoyl dependent decarboxylase, protein self-processing, lyase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm : P0A790 |
Total number of polymer chains | 2 |
Total formula weight | 31955.03 |
Authors | Schmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.,Webb, M.E.,Vinkovic, M.,Matak-Vinkovic, D.,Witty, M.,Chirgadze, D.Y.,Smith, A.G.,Abell, C.,Blundell, T.L. (deposition date: 2003-06-18, release date: 2003-11-18, Last modification date: 2023-08-16) |
Primary citation | Schmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.,Webb, M.E.,Vinkovic, M.,Matak-Vinkovic, D.,Witty, M.,Chirgadze, D.Y.,Smith, A.G.,Abell, C.,Blundell, T.L. Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase Embo J., 22:6193-6204, 2003 Cited by PubMed: 14633979DOI: 10.1093/emboj/cdg575 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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