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. 2011 Nov 7;286(52):45030–45040. doi: 10.1074/jbc.M111.271213

FIGURE 2.

FIGURE 2.

Stereo view of the active site of laminarinase from T. maritima. A, the hydrogen bond network between the active site residues (in yellow) and gluconolactone (in cyan). Hydrogen bonds are shown as dotted lines. B, the inhibitor ctab (in green sticks) is bound in the active site of chain A. In A and B, meshes in orange, blue, and green color represent the difference Fourier map (mFo − DFc) contoured at 4, 3, and 1.5 σ levels, respectively. Gray mesh represents the 2mFo − DFc map contoured at the 1 σ level. C, superposition of TmLamCD structures containing gluconolactone (carbons in cyan) and ctab (carbons in green). Both ligands are shown in ball-and-stick. The molecular surface of the TmLamCD structure is colored by electrostatic potential. Positive and negative values are represented in blue and red, respectively. TmLamCD residues are shown as yellow sticks.