. 2021 Jul 24;19:4156–4164. doi: 10.1016/j.csbj.2021.07.017

Table 1.

Summary of hot residues of caspase-6.

Location	Crucial residues	Refs
L1/60′s helix	Glu53,*Phe55,Phe56, Trp57,His58,Pro62, Glu63, Arg64, Arg65	[22], [29], [27]
L2/L2′	Gln161, Cys163^†, Arg164,*Gly165,His168, Asp179^a, Asp193^a,Leu200	[22], [23]
L3	*Ser211,Val212,Glu214^e,Gly215,Tyr217^e,Ser218*, His219^e, Arg220, Glu221,Thr222,*Val223*, Ser226, Trp227,	[22], [24], [26], [46]
130′s helix	**His121^†*,Gly122^e,**Glu123^e,Gly124,Asn125, His126^e,Ile127,Tyr128*, Asp131^e, Lys133^e, Glu135^b	[23], [26], [29], [45]
Others	Asp23^a, Arg42 ^f, Arg43 ^f, Arg44^f, Lys36^c, Arg65^f, Gly66^f,Ser242, Glu244^c,Thr250, Leu251, Val261,*Leu282, His287^c, Ser257^d	[22], [23], [47], [48], [49]

Bold: 22 crucial residues calculated by PRS (i.e., Phe55, Phe56, His58, Pro62, Gly165, Leu200, Ser211, Val212, Glu214, Gly215, Try217, Ser218, Thr222, Val223, His121, Gly122, Glu123, Gly124, Asn125, His126, Ile127 and Tyr128);

Italic: functional/allosterically relevant residues reported by previous researches;

† Catalytic dyad residues Cys163 and His121;

* Residues within 5 Å of active site;

Residues involved in caspase-6 events of ^a proteolysis, ^b rearrangement of 130′s helix, ^c zinc-mediated allosteric inhibition, ^d phosphorylation-mediated allosteric inhibition, ^e pep419 and Z-VAD-FMK-mediated allosteric inhibition, and ^f mutation-induced allosteric inhibition.