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)

Dali Liu (Contributor)
Edvin V. Pozharski (Contributor)
Bryan W. Lepore (Contributor)
Mengmeng Fu (Contributor)
Richard B Silverman (Contributor)
Gregory A. Petsko (Contributor)
Dagmar Ringe (Contributor)

Dataset

Date made available	Dec 4 2007
Publisher	Protein Data Bank (PDB)

DOI
10.2210/pdb2QB3/pdb

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https://www.wwpdb.org/pdb?id=pdb_00002qb3

1 Article

Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "A tale of two mechanisms"
Liu, D., Pozharski, E., Lepore, B. W., Fu, M., Silverman, R. B., Petsko, G. A. & Ringe, D., Sep 18 2007, In: Biochemistry. 46, 37, p. 10517-10527 11 p.
Research output: Contribution to journal › Article › peer-review
14 Scopus citations

Cite this

Liu, D. (Contributor), Pozharski, E. (Contributor), Lepore, B. W. (Contributor), Fu, M. (Contributor), Silverman, R. B. (Contributor), Petsko, G. A. (Contributor), Ringe, D. (Contributor) (Dec 4 2007). 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). Protein Data Bank (PDB). 10.2210/pdb2QB3/pdb

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)

DOI

Access Dataset

Research output

Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "A tale of two mechanisms"

Cite this