Table 6.
Averages of the binding enthalpy for the amino-acid residues of COX-1 bound to compounds A, B and Ca,2,3.
| Compound | |||
|---|---|---|---|
| Residue of COX-1 | A | B | C |
| Residue Contribution to the Binding Enthalpy (kcal/mol) | |||
| ILE-89 | −1.17 ± 0.50 | – | – |
| LEU-93 | −0.90 ± 0.51 | −0.85 ± 0.37 | – |
| LEU-112 | −0.59 ± 0.48 | −1.02 ± 0.42 | – |
| MET-113 | – | −1.52 ± 0.74 | – |
| VAL-116 | −1.44 ± 0.35 | −1.52 ± 0.40 | −0.74 ± 0.31 |
| LEU-117 | – | −0.80 ± 0.47 | −0.69 ± 0.32 |
| ARG-120 | – | – | −0.54 ± 0.36 |
| ILE-345 | – | – | −0.60 ± 0.50 |
| VAL-349 | −1.90 ± 0.31 | −1.32 ± 0.34 | −1.67 ± 0.34 |
| LEU-352 | −1.86 ± 0.39 | −1.22 ± 0.36 | −1.48 ± 0.33 |
| SER-353 | −0.88 ± 0.33 | −0.70 ± 0.25 | −0.76 ± 0.28 |
| TYR-355 | −1.59 ± 0.68 | −1.15 ± 0.38 | −0.72 ± 0.31 |
| LEU-357 | −0.70 ± 0.52 | −1.09 ± 0.45 | – |
| LEU-359 | −0.48 ± 0.24 | −1.39 ± 0.53 | −0.94 ± 0.27 |
| LEU-384 | – | – | −0.57 ± 0.28 |
| TRP-387 | −0.47 ± 0.24 | – | – |
| PHE-518 | −0.93 ± 0.26 | −0.52 ± 0.26 | −0.87 ± 0.28 |
| MET-522 | – | – | −0.56 ± 0.33 |
| ILE-523 | −2.26 ± 0.64 | −1.16 ± 0.35 | −1.59 ± 0.47 |
| GLY-526 | −0.83 ± 0.26 | −0.50 ± 0.24 | −0.89 ± 0.24 |
| ALA-527 | −1.90 ± 0.33 | −1.34 ± 0.31 | −1.63 ± 0.31 |
| SER-530 | −0.46 ± 0.38 | – | −0.47 ± 0.41 |
| LEU-531 | −0.61 ± 0.27 | −0.56 ± 0.27 | −1.51 ± 0.55 |
aData for the COX-1 residues with the binding enthalpy ≤ −0.4 kcal/mol are presented.
bThe averages of the residue contributions to the binding enthalpy and corresponding standard deviations are given.
cThe COX-1 residues dominating the ligand/protein interaction are highlighted by bold.