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. Author manuscript; available in PMC: 2011 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2009 Aug 4;1800(1):16–22. doi: 10.1016/j.bbagen.2009.07.025

Fig. 4.

Fig. 4

Predicted amino acid sequence of hGSTA5 and its alignment with other human Alpha-class GSTs. The predicted sequence of hGSTA5 is shown in bold type. Underneath that sequence, the remaining human Alpha-class GSTs are listed, with amino acid identities to hGSTA5 shown as dots. The line labeled “A1–A4”, above the hGSTA5 sequence, contains a consensus sequence of hGSTA1, A2, A3, and A4 in which only those residues are shown that are identical in these four proteins. Amino acid residues involved in binding of glutathione (the G-site) are marked with asterisks [on the basis of hGSTA1; ref. 27]. Horizontal lines indicate the three regions in hGSTA1 and hGSTA4 that determine the binding of the electrophilic substrate (the H-site) [29].