Figure 3 | Scientific Reports

Figure 3

From: Structural Insights into Catalytic Versatility of the Flavin-dependent Hydroxylase (HpaB) from Escherichia coli

Figure 3

(a) A superposition of the apo structures of the EcHpaB (cyan) and TtHpaB (coral). The β32-β33 loop is highlighted in dark blue (EcHpaB) and red (TtHpaB). (b) A view of the EcHpaB (cyan) active site. Enzyme-putative FAD hydrogen bonds are denoted by thin black lines while enzyme substrate hydrogen bonds are denoted by red dashed lines. The β32-β33 loop is highlighted in dark blue for EcHpaB and dark coral for TtHpaB. (c) A comparison of the EcHpaB β32-β33 loop structure with that of TtHpaB structures. Blue indicate section I. Red indicate section II and purple indicate section III.

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