5LD0

Chimeric GST

Summary for 5LD0

• Entry DOI: 10.2210/pdb5ld0/pdb
• Descriptor: Glutathione S-transferase A1,Glutathione S-transferase alpha-2,Glutathione S-transferase A1, CHLORIDE ION (3 entities in total)
• Functional Keywords: directed evolution, glutathione transferase a1-1, protein stability, transferase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 25815.59

Authors

Axarli, A.,Muleta, A.W.,Chronopoulou, E.G.,Papageorgiou, A.C.,Labrou, N.E. (deposition date: 2016-06-23, release date: 2016-09-21, Last modification date: 2024-01-10)

Primary citation

Axarli, I.,Muleta, A.W.,Chronopoulou, E.G.,Papageorgiou, A.C.,Labrou, N.E.
Directed evolution of glutathione transferases towards a selective glutathione-binding site and improved oxidative stability.
Biochim. Biophys. Acta, 1861:3416-3428, 2017

PubMed Abstract: Glutathione transferases (GSTs) are a family of detoxification enzymes that catalyze the conjugation of glutathione (GSH) to electrophilic compounds.

PubMed: 27612661
DOI: 10.1016/j.bbagen.2016.09.004

Experimental method

X-RAY DIFFRACTION (1.6 Å)