Skip to main content
. 2016 Sep 19;113(40):11196–11201. doi: 10.1073/pnas.1613630113

Fig. 2.

Fig. 2.

Structural comparison of substrates binding to the active sites of furin and to subtilisin Carlsberg. (A) Structural alignment of selected residues of unliganded furin (yellow carbons) and inhibitor-bound furin (gray carbons; inhibitor: ball-and-stick). Steric clashes between bound inhibitor/substrate and unliganded furin are highlighted as red line patterns. (B) Structural alignment of unliganded subtilisin (orange carbons) and inhibitor-bound subtilisin (green carbons). (C) Structural alignment of inhibitor-bound subtilisin (green carbons) and furin (gray-colored stick model). Important interactions are always highlighted by dashes.