Table 2.

Important residues lining the binding pockets of falcipain-3, falcipain-2, and cathepsin Ka

Subsites	Falcipain-3	Falcipain-2b	Cathepsin Kc
S1	Q45-G49-C89-Y90	Q36-G40-C80-N81	Q19-G23-C63-G64
S2	Y93-I94-S158-P181-E243	L84-I85-S149-L172-D234	Y67-M68-A134-L160-L209
S1′	A160-A161-S162-A166-H183-W215	V150-V152-S153-A157-H174-W206	D136-A137-S138-F142-H162-W184
S3	K85-N86-N87-G91-G92	K76-N77-Y78-G82-G83	E59-N60 -D61-G65-G66

^a The altered residues compared to falcipain-3 are in bold.

^bBased on the homology model of falcipain-2 (Sabnis et al. 2002).

^c The residues are numbered as in 1ATK.pdb.