A single water molecule guarantees this protein's rigidity by linking two isoleucine residues at positions 50 and 150.
A single water molecule guarantees this protein's rigidity by linking two isoleucine residues at positions 50 and 150. The two identical subunits of this protein have glycine-rich folds nicknamed "flaps" due to this protein's shocking resemblance to the face of a bulldog.  A very strong binder to this enzyme contains two fused THF rings on one end. This protein, which does not bind a nucleic acid, commonly accumulates the V82A and I84V mutations according to a database kept by (*) Stanford. Hydroxyethylamine is a transition state mimic for this protein. Inhibitors of this protein can cause odd lipodystrophies like a Crix belly. 1996 Time Man of the Year David Ho pioneered inhibitors of this enzyme like saquinavir. This protein has an aspartate-threonine-glycine catalytic triad, which it uses to break apart the Gag and Pol polyproteins. For 10 points, name this enzyme that hydrolyzes peptide bonds, extracted from the virus that causes AIDS.
A single water molecule guarantees this protein's rigidity by linking two isoleucine residues at positions 50 and 150.
HIV-1 protease [or HIV-1 proteinase; or HIV-1 peptidase; or retropepsin; prompt on partial answer]