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. Author manuscript; available in PMC: 2009 Nov 25.
Published in final edited form as: Apoptosis. 2008 Nov;13(11):1291–1302. doi: 10.1007/s10495-008-0259-9

Fig. 3.

Fig. 3

Overall structure of caspase-3/LDESD. Two heterodimers (p17/p12)2 of caspase-3/LDESD are shown in a ribbon representation with the large and small subunits colored cyan and pink, respectively. The inhibitor Ac-LDESD-CHO is colored by element type. The side chains of caspase-3 residues that interact with P5 Leu are shown in red. The N and C termini are indicated for the 12 kDa and 17 kDa chains. L1 to L4 indicate loops 1 to 4 that form the substrate binding site.