5AGY

CRYSTAL STRUCTURE OF A TAU CLASS GST MUTANT FROM GLYCINE

Summary for 5AGY

• Entry DOI: 10.2210/pdb5agy/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, 4-NITROPHENYL METHANETHIOL, S-(P-NITROBENZYL)GLUTATHIONE, ... (5 entities in total)
• Functional Keywords: transferase, binding site, catalytic domain, enzyme, induction, detoxification, herbicides, kinetics, site-directed mutagenesis, soy beans, glutathione transferase, protein stability, catalytic mechanism, xenobiotic binding, allosterism
• Biological source: GLYCINE MAX (SOYBEAN)
• Total number of polymer chains: 2
• Total formula weight: 52696.64

Authors

Axarli, I.,Muleta, A.W.,Vlachakis, D.,Kossida, S.,Kotzia, G.,Dhavala, P.,Papageorgiou, A.C.,Labrou, N.E. (deposition date: 2015-02-04, release date: 2015-12-16, Last modification date: 2024-01-10)

• Primary citation: Axarli, I.,Muleta, A.W.,Vlachakis, D.,Kossida, S.,Kotzia, G.,Maltezos, A.,Dhavala, P.,Papageorgiou, A.C.,Labrou, N.E.; Directed Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity.; Biochem.J., 473:559-, 2016; PubMed: 26637269; DOI: 10.1042/BJ20150930

Experimental method

X-RAY DIFFRACTION (1.75 Å)