2QB3
Structural Studies Reveal the Inactivation of E. coli L-Aspartate Aminotransferase by (s)-4,5-dihydro-2-thiophenecarboxylic acid (SADTA) via Two Mechanisms (at pH 7.5)
Summary for 2QB3
Entry DOI | 10.2210/pdb2qb3/pdb |
Related | 2Q7W 2QA3 2QB2 |
Descriptor | Aspartate aminotransferase, SULFATE ION, 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]THIOPHENE-2-CARBOXYLIC ACID, ... (6 entities in total) |
Functional Keywords | mechanism-based inactivator, ph dependence, aspartate aminotransferase, sadta, plp, transferase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P00509 |
Total number of polymer chains | 1 |
Total formula weight | 45203.60 |
Authors | Liu, D.,Pozharski, E.,Lepore, B.,Fu, M.,Silverman, R.B.,Petsko, G.A.,Ringe, D. (deposition date: 2007-06-15, release date: 2007-12-04, Last modification date: 2011-07-13) |
Primary citation | Liu, D.,Pozharski, E.,Lepore, B.W.,Fu, M.,Silverman, R.B.,Petsko, G.A.,Ringe, D. Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms". Biochemistry, 46:10517-10527, 2007 Cited by PubMed: 17713924DOI: 10.1021/bi700663n PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report