International Journal of Evolutionary Biology / 2009 / Article / Fig 4

Research Article

Divergence of AMP Deaminase in the Ice Worm Mesenchytraeus solifugus (Annelida, Clitellata, Enchytraeidae)

Figure 4

Four sterically constraining residues (K173, Y174, D444 and D445) define the surface area of the AMPD substrate binding plane as ~38       in A. thaliana (a), ~36    in A. thaliana K188E (b), ~36      in the ice worm E188 (c), and predicted loss of structure in ice worm E188K (d). Position 188 is visible to the right in each panel.

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