The active site is located in an hydrophobic pocket.
One end of the channel is open to the cytosol, whereas the other end forms a hydrophobic pocket.
The 9 - N butyl chain occupy the lateral hydrophobic pocket.
A deep hydrophobic pocket is formed at the interface of these subdomains.
The M site is placed at the bottom of the hydrophobic pocket with several metal atoms.
Pleconaril binds to a hydrophobic pocket in the VP1 protein.
The organic substituents also define a hydrophobic pocket around the reactive coordination site.
These attempted to recreate haemoglobin's hydrophobic pocket on one side of the iron complex.
Instead, a hydrophobic pocket was proposed to exist in the vicinity of the C-2 carbon.
The sequence binds to the hydrophobic pocket of the SH3 domain.
