When the anomeric hydroxyl of a D-hexose is on the same side of the ring as C-6, the structure is β a by definition; when it is on the opposite side from C-6, the structure is α.

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In unstimulated cells, 

concentration of phosphoinositides is low, and PKB is

inactive because its PH domain physically blocks the kinase active site

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Ligand-induced receptor activation,

Concentration of PI 3-phosphates rises

PH domain of PKB binds to PI 3-phosphates

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Maximal activation of PKB depends on recruitment to the cytosolic surface of the plasma membrane of two other kinases -PDK1 and PDK2.

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PDK1 can phosphorylate PKB on a critical threonine residue in its activation loop

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Phosphorylation by the mTORC2 kinase complex, of a second serine on

PKB that is not in the activation loop is necessary for maximal PKB activity

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Activated PKB directly phosphorylates and inactivates a protein Bad