2QB2

Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).

Summary for 2QB2

Entry DOI	10.2210/pdb2qb2/pdb
Related	2Q7W 2QA3 2QB3
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	45664.07
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: 2023-08-30)
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: 17713924 DOI: 10.1021/bi700663n PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation