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 Cited by PubMed: 26637269DOI: 10.1042/BJ20150930 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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