Figure 3.
Fig. 3. Superposition of the 187-209 loop of the
wild-type 17 -HSD1 model
(1bhs (24)) (medium gray) and the monomer mC of the
H221L·E2·NAD^+ complex (black) with the 182-203
loop of the MLCR model (1cyd (22)) (light gray). Phe^192 of the
H221L mutant and Met186 of MLCR superpose very well and make
extensive hydrophobic contacts with the nicotinamide ring.
Lys195 of the H221L model interacts with the 2'-phosphate while
no equivalent residue is found for MLCR.
-HSD1 model
(1bhs (24)) (medium gray) and the monomer mC of the
H221L·E2·NAD^+ complex (black) with the 182-203
loop of the MLCR model (1cyd (22)) (light gray). Phe^192 of the
H221L mutant and Met186 of MLCR superpose very well and make
extensive hydrophobic contacts with the nicotinamide ring.
Lys195 of the H221L model interacts with the 2'-phosphate while
no equivalent residue is found for MLCR.