Figure 2 | Scientific Reports

Figure 2

From: Determinants of ligand binding and catalytic activity in the myelin enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Figure 2

Inactivating mutations.

(a) Superposition of all His230 and His309 mutant structures shows minimal molecular rearrangement within the active site. The additional water molecule that partially substitutes for the absent His309 imidazole in the H309S substrate complex structure is indicated (blue). (b) Superposition of Phe235 mutants with the H309S substrate complex demonstrates minimal molecular rearrangement in the active site, despite almost complete inactivation. (c) Mutations in Tyr168 result in minor molecular rearrangements in the active site, most notably at position 168, as well as at Pro225 and His230.

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