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. 2014 Dec 8;9(12):e113773. doi: 10.1371/journal.pone.0113773

Table 2. Amino acid residues of AK which form important non-covalent interactions required for the conformational stability of the receptor and binding of inhibitors.

S No	Non-covalent interactions	G-loop	DFG-loop	A-loop	αC-helix	Hinge
1.	π-systems:	F144^G-loop	F275^DFG-loop	W277^A-loop	Y246	Y212^Hinge
	Aromatic residues	Y148^G-loop	F144^G-loop	F275^DFG-loop	F165	F144^G-loop
	(Phe, Tyr, Trp)	F275^DFG-loop	W277^A-loop	Y246	Y199	Y197
			Y246		Y207	Y246
					F200
2.	Cationic-systems:	R195	K162	R255^HRD	K166 ^αC-helix	R195
	Positively charged R-groups	R189		R180^HRD	R179^αC-helix	R189
	(Lys, Arg)				R205	R137
					R189
3.	Salt-bridge:	E211^Hinge	-	E260	E181^αC-helix	E211^Hinge
	Anionic carboxylate (RCOO^-)	E260
	Negatively charged R-groups
	(Asp, Glu)
	Cationic ammonium (RNH₃ ⁺)	K143^G-loop		R285^A-loop	K162	K145^G-loop
	of Lys and guanidinium	K141^G-loop		K309	R195	K141^G-loop
	(RNHC(NH₂)₂ ⁺) of Arg					K271