The average RMSD of the full complex wild-type PrnA is 3.5 Å and in the apoenzyme PrnA is 3.6 Å, indicating a slight trend of increased flexibility of the apoenzyme form possibly due to the absence of bound ligands.
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Structural Insights from Molecular Dynamics Simulations of Tryptophan 7-Halogenase and Tryptophan 5-Halogenase.
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