Figure 5
From: A novel method to compare protein structures using local descriptors
Alignment of the Saposin domain of NK-lysin and the "swaposin" domain of prophytepsin. (a) The Saposin domain of NK-lysin (SCOP domain d1nkla_) and (b) the "swaposin" domain of prophytepsin (d1qdma1). Despite different topology these two domains have the same architecture and identical disulfide bonds. (c) DEDAL correctly identifies the best superposition and the disulfide bond network (the sequence identity between these molecules is 14.5%).