Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site

• Main Authors: Wongsantichon, J, Robinson, R.C, Ketterman, A.J
• Other Authors: CHEMICAL & BIOMOLECULAR ENGINEERING
• Format: Article
• Published: Portland Press Ltd 2020
• Subjects: glutathione; glutathione transferase; glutathione transferase E6; histidine; serine; unclassified drug; Drosophila protein; GSTE6 protein, Drosophila; amino acid sequence; Article; binding affinity; controlled study; crystal structure; Drosophila melanogaster; enzyme specificity; molecular interaction; nonhuman; protein folding; protein quaternary structure; protein subunit; residue analysis; sequence alignment; sequence analysis; structure activity relation; structure analysis; animal; binding site; chemistry; enzyme active site; enzymology; genetics; metabolism; protein conformation; protein motif; X ray crystallography; Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Drosophila Proteins; Glutathione; Glutathione Transferase; Protein Conformation
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/179632
• Institution: National University of Singapore

10.1042/BSR20150183