Figure 4
Figure 4. Binding interfaces for warfarin on hVKORC1 in relation to OACR mutations. (A) A close-up view of the 3 putative wafarin binding interfaces of hVKORC1 for the position with the best pseudo-energy docking score. The putative warfarin binding interfaces are highlighted by blue boxes and identified by roman numerals; (I), (II) and (III) indicate the first, second, and third binding interfaces, respectively. Reported human mutations influencing each interface are depicted as stick diagrams in gray color. The conserved loop and CXXC motif cysteine residues are represented in yellow stick form. The protein backbone is depicted in ribbon format. The warfarin molecule is represented by its solvent accessible surface area (colored red). (B) The horizontally opposite view of panel A showing the mutations (in blue box) that are distant to the 3 putative binding interfaces located in the membrane embedded segment of the loop.

Binding interfaces for warfarin on hVKORC1 in relation to OACR mutations. (A) A close-up view of the 3 putative wafarin binding interfaces of hVKORC1 for the position with the best pseudo-energy docking score. The putative warfarin binding interfaces are highlighted by blue boxes and identified by roman numerals; (I), (II) and (III) indicate the first, second, and third binding interfaces, respectively. Reported human mutations influencing each interface are depicted as stick diagrams in gray color. The conserved loop and CXXC motif cysteine residues are represented in yellow stick form. The protein backbone is depicted in ribbon format. The warfarin molecule is represented by its solvent accessible surface area (colored red). (B) The horizontally opposite view of panel A showing the mutations (in blue box) that are distant to the 3 putative binding interfaces located in the membrane embedded segment of the loop.

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