Protein Structure from Scientific Research

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Overview of the lipase domain ( i ) and expanded view of the catalytic site ( ii ) of cPGAP1 apo . Elements including the central -sheet (strands 1-8) (orange), the sandwiching -helices (yellow), the nucleophilic elbow (green), the catalytic triad (cyan), the backbone nitrogen of the oxyanion hole (blue) are highlighted. Palmitic acid (PLM, green), and the manually fitted GPI-AP 3 (only showing relevant parts, purple) (Fig. S9 ) are superimposed to illustrate the proposed substrate positioning. Numbers indicate distances () either observed structurally (black) or measured from superposed ligands (magenta).
#Protein Structure#Chemical Structure#Lipase Domain#Catalytic Site#cPGAP1 apo#Beta-sheet#Alpha-helices#Nucleophilic Elbow#Catalytic Triad#Oxyanion Hole#Palmitic Acid#GPI-AP
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