Figure 6. The secondary and tertiary structure of human 11β-hydroxysteroid dehydrogenase type 1.
Figure 7. Overlay of NADP(H) molecules.
Figure 8. The hydrogen bonds between 11β-hydroxysteroid dehydrogenase type 1 and NADP(H) for the 2ILT structure.
Figure 9. The possible hydrogen bonds between the protein, ligand (9) and cofactor in the 1XU7_a structure.
Figure 10. The interactions between 2-(
N
-morpholino)-ethanesulfonic acid (10) and 1XU9_a and 1XU9_b.
Figure 11. The possible hydrogen bonds between the protein, ligand (11) and cofactor in the 2BEL_a structure.
Figure 12. The possible hydrogen bonds between the protein, ligand (12) and cofactor in the 2ILT structure.
Figure 13. The possible hydrogen bonds between the protein, ligand (14) and cofactor in the 3BYZ_a structure.
Figure 14. The possible hydrogen bonds between the protein, ligand (17) and cofactor in the 2RBE_a structure.
Figure 15. The possible hydrogen bonds between the protein, ligand (19) and cofactor in the 3D5Q_a structure.
Figure 16. The possible hydrogen bonds between the protein, ligand (20) and cofactor in the 3ZCR_a structure.
Figure 17. The possible hydrogen bonds between the protein, ligand (22) and cofactor in the 3HFG_a structure.
Figure 18. The possible hydrogen bonds between the protein, ligand (24) and cofactor in the 3FRJ_b structure.
Figure 19. The water-mediated hydrogen bond network along the NADP(H) binding site in the 3FRJ_b structure.
Figure 21. Differences between the human and guinea pig interactions with NADP(H).
Figure 22. Differences in the substrate binding sites of 1XSE_a (guinea pig) and 2ILT (human).
Figure 23. Differences in the substrate binding sites of the human and mouse enzymes.
Figure 24. Overlay of the Cα trace of those residues that form the opposing walls of substrate binding site showing the variability in the flexible loop.
Figure 25. The substrate binding site ligands.