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. 2012 Jul 19;10(7):1545–1565. doi: 10.3390/md10071545

Table 3.

The amino acid residues’ contribution to binding free energies and interfaces for the complexes of inhibitors with trypsin. Amino acid residues making the greatest contribution to binding free energy are highlighted in light green.

Reactive site Weak contact site
BPTI (3OTJ) Pro12 Cys13 Lys14 Ala15 Arg16 Cys37 Arg38 Lys45
ΔGbind, Kcal/Mol −2.1 −4.8 −8.1 −3.3 −3.2 −1.8 −2 1.1
ΔSASA, Ǻ2 33 51.6 165.2 36 110.8 27.2 97.2 0
BPTI mutant (3BTT) Pro12 Cys13 Thr14 Ala15 Arg16 Cys37 Arg38 Lys45
ΔGbind, Kcal/Mol −2.1 −4,6 −4.4 −3.5 −3.5 −1.7 −1.6 0.3
ΔSASA, Ǻ2 37.9 55.5 101.4 36.5 118.3 28.6 94.6 0
SHPI-1 (3M7Q) Arg12 Cys13 Lys14 Gly15 Tyr16 Cys37 Gly38 Glu45
ΔGbind, Kcal/Mol −3.4 −2.9 −8.4 −2.2 −4.5 −1.4 −0.1 −0.5
ΔSASA, Ǻ2 143.8 52 163.6 19.9 88.7 30 0.9 0
InhVJ Pro12 Cys13 Thr14 Ala15 Tyr16 Cys37 Glu38 Glu45
ΔGbind, Kcal/Mol −2.1 −4.4 −4.7 −2.6 −5.9 −1.1 −0.2 −8.4
ΔSASA, Ǻ2 50.5 53 106.1 30.5 102.2 37.2 0 37.9