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. 2000 Jul 18;97(17):9408–9412. doi: 10.1073/pnas.150084897

Figure 1.

Figure 1

The three hydrophobic substrate-binding modules of human GST A1–1 (2) and human GST A4–4 (17): the β1-α1 loop (residues 9–16), the C-terminal part of the α4 helix (residues 104–111), and the C terminus of the protein (residues 208–222, where 210–220 form the α9 helix). GST A4–4 residues considered important for proper first-sphere interactions with alkenal substrates and installed into corresponding positions in GST A1–1 are boxed. Residue numbers are indicated above the residues at each end.