Table 4 In silico molecular docking parameters between the ligands (conoidecyclics A-C) and the amino acyl residues at the active sites of COX-2, 5-LOX, PTP-1B and ACE.
Molecular docking parameters against COX-2

a Molecular docking simulations were carried out using Autodock 4 software tool.

b Values were evaluated from the calculations based on the energy minimization.
a Ligands b Binding energy (kcal mol 1) b Docking score (kcal mol 1) b Inhibition constant, Ki (pM) b Intermolecular energy (kcal mol 1) b Torsional free energy (kcal mol 1) Hydrogen bonded residues H-bond length (Å)
Conoidecyclic 14.51 15.45 23.20 15.46 1.49 GLU 81.A, SER 34.A, 2.55, 2.95,
A GLN 447.A 3.10
Conoidecyclic 12.93 12.95 30.55 12.93 0.95 ASN 368.A, THR 198.A 3.14, 2.63
B
Conoidecyclic 10.24 10.82 31.94 11.04 0.90 TYR 108.A 3.07
C
Molecular docking parameters against 5-LOX
Conoidecyclic 13.34 14.56 33.23 14.12 1.19 ARG 666.B, GLU 614.B 2.81, 2.51
A
Conoidecyclic 10.75 11.25 53.25 11.32 0.91 ILE 406.B 2.65
B
Conoidecyclic 9.70 10.10 77.21 10.03 0.60 GLN 363.B 2.83
C
Molecular docking parameters against PTP-1B
Conoidecyclic 13.87 14.55 42.15 14.82 1.29 PHE 95.A, GLU 97.A, 2.35, 3.21,
A GLN 85.A, ARG 43.A 1.87, 1.84,
1.98
Conoidecyclic 11.61 12.85 55.18 12.81 0.97 GLU 101.A 3.13
B
Conoidecyclic 11.04 12.12 57.62 11.98 0.88 ALA 262.A, TYR 20.A, 2.57, 2.61,
C GLY 259.A 2.63
Molecular docking parameters against ACE
Conoidecyclic 11.27 12.42 55.31 12.46 1.49 GLU 376.A, ASP 415.A, 2.84, 2.93,
A HIS 353.A 2.85
Conoidecyclic 9.24 10.29 59.78 10.33 1.31 GLN 281.A, PHE 527.A 2.97, 2.59
B
Conoidecyclic 8.44 9.95 68.22 9.91 1.11 – –
C