Fig. 1From: Molecular dynamics and structure function analysis show that substrate binding and specificity are major forces in the functional diversification of EqolisinsStructure of SCP-B Eqolisin. Eqolisins consist of two pleated β-sheets (Cyan and green for inner and outer sheet, respectively) that fold into a double convex halfpipe. E136 and Q53 (red licorice) stick into the binding cleft and form the catalytic site. The β-loop (purple) and 70’s-loop (yellow) have been shown to migrate inwards during substrate bindingBack to article page