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Figure 1. The Reaction Catalyzed by Human HMG-CoA Reductase
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Figure 2. Tetrameric Structure of Human HMG-CoA Reductase
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Figure 3. Structure of Human HMG-CoA Reductase as a Dimer of Dimers
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Figure 4. One Dimer of Human HMG-CoA Reductase with HMG and Catalytic Sites
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Figure 5. Secondary Structures in one Monomer of Human HMG-CoA Reductase
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Figure 6. The Domains highlighted in one Monomer of Human HMG-CoA Reductase
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Figure 7. The "Cis-Loop" in one Monomer
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Figure 8. The residues of the Cis-Loop
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Figure 9. A Salt Bridge between E730 of one Monomer and R595 of another Monomer
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Figure 10. H-bonds between E700 residues on neighboring monomers stabilize the HMGR tetramer_images/img_3_11.png)
Figure 11. A Salt Bridge between residues R641 and E782 stabilizes the dimer-dimer interface
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Figure 12. The Phosphorylation Site and N-terminus of Human HMG-CoA Reductase-- Residue S872
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Figure 13. The NADP(H) Binding Pocket
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Figure 14. Binding of a section of NADP(H) to residues 626-628 of Human HMGR
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Figure 15. Binding of NADP(H) to residues N870 and R871 of Human HMGR
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Figure 16. The Coenzyme A Binding Pocket
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Figure 17. Y479 stabilizes Coenzyme A binding via hydrophobic interactions
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Figure 18. The HMG Binding Pocket
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Figure 19. Residues C688 and T689 of the Cis-Loop with HMG
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Figure 20. The positively charged K691 Residue with Coenzyme A
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Figure 21. Proton Donors E559 and H866 with HMG in the active site of HMGR
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Figure 22. The binding pocket of Rovustatin to Human HMGR
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Figure 23. The unique polar interactions of Rovustatin's sulfone group with residues R568 and S565
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Figure 24. Superimposition of one dimer of Human HMGR with the dimeric HMGR from the bacterium P. mevalonii