
-   Protein Accession: P09211
-   Size: 210 amino acids
-   Molecular mass: 23356 Da
-   Domains: Thioredoxin-like_sf, Glutathione-S-Trfase_C_sf, GST_C, Glutathione-S-Trfase_C-like, Glutathione_S-Trfase, Glutathione_S-Trfase_N, GST_pi
-   Blocks: Glutathione S-transferase, N-terminal, Alpha-class glutathione S-transferase signature, Pi-class glutathione S-transferase signature
-   Family: Belongs to the GST superfamily. Pi family.
-   The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Pi GST is a homodimeric eukaryotic protein. The GST active site is composed of a GSH binding site (G-site), common to all GSTs, and a xenobiotic binding site (H-site), which varies between different classes and isotypes. Residues from the N-terminal TRX-fold domain form the G-site while the H-site is comprised mainly of residues from the C-terminal alpha helical domain. [[https://www.uniprot.org/uniprotkb/P46425/entry#family_and_domains](https://www.uniprot.org/uniprotkb/P46425/entry#family_and_domains)]
-   In addition to a TATA box and a sequence motif matching the phorbol-ester-responsive element, the promoters of Gst p-2 exhibit two G+C boxes (GGGCGG) [PMID: 8135745].
