Structure
| Glutathione S-transferase, C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Structure of the xenobiotic substrate binding site of rat glutathione S-transferase mu 1 bound to the GSH adduct of phenanthrene-9,10-oxide. | |||||||||
| Identifiers | |||||||||
| Symbol | GST_C | ||||||||
| Pfam | PF00043 | ||||||||
| InterPro | IPR004046 | ||||||||
| SCOP | 2gst | ||||||||
| SUPERFAMILY | 2gst | ||||||||
| CDD | cd00299 | ||||||||
|
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Mammalian cytosolic GSTs are dimeric both subunits being from the same class of GSTs, although not necessarily identical. The monomers are in the range of 22–30 kDa. They are active over a wide variety of substrates with considerable overlap.
Read more about this topic: Glutathione S-transferase
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