Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors

Table 2 The percent of the total enzyme buried area occupied by amino acid sub-classes

Inhibitor bound to serine proteases		[%] Hydrophobic residues in buried area	[%] Charged residues in buried area	[%] Polar residues at buried area (glycine %)	[%] (Charged + Polar) residues in buried area
BPTI	Trypsin (9)	14	10	76 (10)	86
	Chymotrypsin (4)	35	11	54 (8)	65
	Elastase (5)	25	21	54 (6)	75
	Thrombins (5)	16	37	47 (6)	84
Ecotine	Trypsin (9)	13	15	72 (10)	87
	Chymotrypsin (4)	30	18	52 (6)	70
	Elastase (5)	22	19	59 (9)	78
	Thrombins (5)	12	53	35 (6)	88
Ovomucoid Third domain	Trypsin (9)	12	10	78 (11)	88
	Chymotrypsin (4)	32	10	58 (9)	68
	Elastase (5)	24	20	56 (9)	86
	Thrombins (5)	15	37	48 (7)	85

The serine proteases are bound to BPTI, ecotine and ovomucoid third domain inhibitors. Areas occupied by the three classes of amino acids, with respect to the total buried enzyme area, are expressed as a percentage. The numbers between the brackets show the number of enzyme - inhibitor complexes included in this analysis for each subfamily. The column containing polar residue participation also contains (within brackets) the participation of glycine residues.

ISSN: 1472-6807