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Exact(2)
The binding pocket is indicated as an exclusion surface.
The green protein residues belong to L A and the orange ones to L B. The binding pocket is indicated as an exclusion surface.
Similar(58)
RNA binding groove and hydrophobic pocket are indicated by arrow.
From the chemistry point of view the aldose sugar moiety could be replaced with some five-membered heterocycles (compounds 1 3) or fused five/six-membered rings (compounds 12 and 13) indicating that the binding pocket is large enough to accommodate these types of structures.
These results indicate that the CYP3A4 binding pocket is large enough to accommodate up to four CBZ molecules and that the A370V and I369F mutations considerably affect the mobility of CBZ molecules bound in the binding pocket.
The positively charged binding pocket is not big enough for ANP binding.
Moreover, a new binding pocket is also explored.
Replacement of water from the uncomplexed binding pocket is assumed to be entropically favorable.
Docked ligand conformation, is presented with sticks and the binding pocket is shown as surface.
The negatively charged binding pocket is not big enough for ATP (Fig. 2B).
The volume of the binding pocket is 495 Å.
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