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2QA3

Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via two mechanisms (at pH6.5)

Summary for 2QA3
Entry DOI10.2210/pdb2qa3/pdb
Related2Q7W
DescriptorAspartate 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 Keywordsplp, sadta, asparate aminotransferase, mechanism-based inhibitor, e. coli, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm: P00509
Total number of polymer chains1
Total formula weight45852.23
Authors
Liu, D.,Pozharski, E.,Lepore, B.,Fu, M.,Silverman, R.B.,Petsko, G.A.,Ringe, D. (deposition date: 2007-06-14, release date: 2007-12-04, Last modification date: 2023-08-30)
Primary citationLiu, 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 (1.75 Å)
Structure validation

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