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The side chains of Val, ΔPhe and Ile form infinite chains of van der Waals interactions.
Glu117 and His88 make strong hydrogen bonds with the adenine base of the DCoA molecule in hydrophobic contact with the side chains of Val 91, Ile 112.
Figure 6B shows that the side chains of Val and Tyr in Lqq III (an anti-insect α-toxin) are largely buried in the molecular core.
A small cavity lies beneath the indole ring in the wild-type structure, and the nearby side chains of Val, Val, Leu and Val were essentially unperturbed by the rotation of the indole ring.
The aromatic rings of Tyr, Phe, Phe and Phe and the side chains of Val and Ile form the walls of the active-site cleft surrounding the Trp ring.
The higher thermal stability of the A441V and A441I mutants relative to that of the wild-type and A441C, A441S, and A441T is consistent with the extensive interactions made by the side chains of Val and Ile, as indicated by our models and the known crystal structures of ALDH10 enzymes that contain Ile at this position, and with the hydrophobicity of these two residues.
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CEO of Professional Science Editing for Scientists @ prosciediting.com