1QIS
ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191F MUTATION, WITH BOUND MALEATE
Summary for 1QIS
Entry DOI | 10.2210/pdb1qis/pdb |
Related | 1QIR 1QIT |
Descriptor | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, MALEIC ACID, ... (4 entities in total) |
Functional Keywords | aminotransferase, transferase(aminotransferase), pyridoxal phosphate, maleate |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm: P00509 |
Total number of polymer chains | 1 |
Total formula weight | 44026.46 |
Authors | Jeffery, C.J.,Gloss, L.M.,Petsko, G.A.,Ringe, D. (deposition date: 1999-06-15, release date: 2000-06-05, Last modification date: 2023-12-13) |
Primary citation | Jeffery, C.J.,Gloss, L.M.,Petsko, G.A.,Ringe, D. The Role of Residues Outside the Active Site in Catalysis: Structural Basis for Function of C191 Mutants of E. Coli Aspartate Aminotransferase Protein Eng., 13:105-, 2000 Cited by PubMed: 10708649DOI: 10.1093/PROTEIN/13.2.105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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