Fig. 2: Root-mean-square fluctuation (RMSF) and H-bond interactions in computational models of HvExoI wild-type (WT) and E220A covalent complexes. | Communications Biology

Fig. 2: Root-mean-square fluctuation (RMSF) and H-bond interactions in computational models of HvExoI wild-type (WT) and E220A covalent complexes.

From: The structure and dynamics of water molecule networks underlie catalytic efficiency in a glycoside exo-hydrolase

Fig. 2

a RMSF values (Å) are specified as the average of three replicates. Panels indicate RMSF values and their differences along protein chains, respectively. Loops carrying E220 (E220A) residues in 220–226 regions, and E491 residue in 494–497 regions of WT (cartoons, cpk sticks) and E220A (cartoons, magenta cpk sticks) covalent complexes. W286, W434, D285, L5 and D285-Glc adduct (cpk sticks) are shown for WT. Separations (Å) between Cα atoms of E220 (E220A) and E491 residues are indicated in dashed lines. Properties of surface morphologies coloured by electrostatic potentials are described in Fig. 1. Subsites −1, +1 and +2 are marked. Selected Glc moieties of L5 are displayed. b Active site residues-solute H-bond interactions. c Active site residues-solvent (water molecules) (SolventAcc) and donor residues-solvent (SolventDnr) H-bond interactions, calculated by cpptraj80. H-bond fractional occupancy heat term is given as the average of three replicates.

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