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Figure 4.
Figure 4. Stereo view of the atomic interactions between GA and
substrate. Displayed are interactions between GA and the bound
substrate molecule NAcGlc-Asn at the active site A. The active
side-chain conformation of residue Cys152 is shown in magenta
and the switch between its inactive trans- and active gauche(+)
conformations is indicated by the magenta double arrow.
Nucleophilic attack is indicated by the green straight arrow. A
candidate water molecule to protonate the leaving group is also
shown (W). The green dotted lines indicate possible
hydrogen-bonding interactions between Cys152 and the surrounding
residues. The blue dotted lines denote other hydrogen bonds
involved in enzyme–substrate binding. Also shown is a hydrogen
bond (a black dotted line) between side-chains of Trp11 and
Thr203. Key active site residues are shown by atom type: yellow
for carbon, blue for nitrogen, red for oxygen, and green for the
Cys152 sulfur atom. The salt bridge is indicated by the
positive and the negative charges. Figure 4. Stereo view of
the atomic interactions between GA and substrate. Displayed are
interactions between GA and the bound substrate molecule
NAcGlc-Asn at the active site A. The active side-chain
conformation of residue Cys152 is shown in magenta and the
switch between its inactive trans- and active gauche(+)
conformations is indicated by the magenta double arrow.
Nucleophilic attack is indicated by the green straight arrow. A
candidate water molecule to protonate the leaving group is also
shown (W). The green dotted lines indicate possible
hydrogen-bonding interactions between Cys152 and the surrounding
residues. The blue dotted lines denote other hydrogen bonds
involved in enzyme–substrate binding. Also shown is a hydrogen
bond (a black dotted line) between side-chains of Trp11 and
Thr203. Key active site residues are shown by atom type: yellow
for carbon, blue for nitrogen, red for oxygen, and green for the
Cys152 sulfur atom. The salt bridge is indicated by the positive
and the negative charges.
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