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. 2019 Jul 3;9:9630. doi: 10.1038/s41598-019-45883-9

Table 6.

Interacting residues of ERK with Dactinomycin, Bromocriptine, Temsirolimus, Everolimus, and Docetaxel.

Drugs Binding Affinity (−log10(KD|Ki)) Protein Residue Distance (Å) Type of Interactions
Dactinomycin 37.7 ILE 31 3.63 Hydrophobic
ALA 35 3.61 Hydrophobic
TYR 36 3.96 Hydrophobic
VAL 39 3.53 Hydrophobic
GLU 53 3.49 H-bond
ARG 67 2.18 H-bond
LYS 151 4.00 Salt bridge
Bromocriptine 32.7 VAL 39 3.47 Hydrophobic
ALA 52 3.71 Hydrophobic
LYS 54 3.88 Hydrophobic
ILE 84 3.06 Hydrophobic
LEU 156 3.97 Hydrophobic
TYR 36 2.08 H-bond
GLY 37 3.45 H-bond
LYS 54 2.17 H-bond
ASP 167 2.74 H-bond
ASP 111 3.15 Halogen bond
LYS 114 3.92 Halogen bond
ARG 67 4.55 Salt bridge
Temsirolimus 37.8 TYR 36 3.51 Hydrophobic
VAL 39 3.34 Hydrophobic
TYR 113 3.97 Hydrophobic
LEU 156 3.70 Hydrophobic
GLU 33 3.07 H-bond
LYS 54 2.42 H-bond
ARG 67 3.11 H-bond
GLU 71 2.55 H-bond
SER 153 2.98 H-bond
LYS 114 5.29 Salt bridge
LYS 151 3.93 Salt bridge
Everolimus 41.2 VAL 39 3.49 Hydrophobic
LEU 170 3.72 Hydrophobic
GLU 33 2.89 H-bond
TYR 36 1.83 H-bond
LYS 54 2.68 H-bond
TYR 64 3.08 H-bond
GLU 71 1.90 H-bond
ASP 167 3.31 H-bond
LYS 151 3.21 Salt bridge
Docetaxel 38.3 ILE 31 3.54 Hydrophobic
ALA 35 3.76 Hydrophobic
TYR 36 3.83 Hydrophobic
VAL 39 3.50 Hydrophobic
ALA 52 3.59 Hydrophobic
ILE 56 3.49 Hydrophobic
TYR 64 3.67 Hydrophobic
ILE 84 3.26 Hydrophobic
LEU 156 3.49 Hydrophobic
ALA 35 3.09 H-bond
LYS 54 2.73 H-bond
LYS 151 2.21 H-bond
ASN 154 3.42 H-bond
ASP 167 2.57 H-bond
LYS 54 5.04 Salt bridge
ARG 67 4.76 Salt bridge