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. 2023 Jul 18;13(8):277. doi: 10.1007/s13205-023-03677-x

Table 2.

Interaction profiling of FIKK9.1 with its natural ligand (ATP) and inhibitors (Compound 1/2)

Compound Residue number AA Distance (Å) Donor atom Acceptor atom Interaction type
1 243 PHE 3.55 5576 2444 Hydrophobic
250 LEU 3.56 5570 2501 Hydrophobic
314 LEU 3.02 5567 3129 Hydrophobic
366 GLU 3.38 5579 3676 Hydrophobic
369 LEU 3.32 5564 3707 Hydrophobic
369 LEU 3.28 5565 3708 Hydrophobic
443 ILE 3.34 5578 4467 Hydrophobic
367 ASN 2.83 5560 3687 Hydrogen bonding
318 ASP 5.38 5558 Salt bridge
2 250 LEU 3.08 5574 2501 Hydrophobic
261 THR 3.46 5574 2612 Hydrophobic
295 ILE 3.25 5572 2959 Hydrophobic
318 ASP 3.53 5581 3164 Hydrophobic
366 GLU 3.08 5579 3676 Hydrophobic
369 LEU 3.31 5571 3707 Hydrophobic
369 LEU 3 5567 3708 Hydrophobic
ATP 242 ASN 1.71 2431 5561 Hydrogen bonding
263 LYS 3.09 2630 5572 Hydrogen bonding
315 TYR 2.67 3132 5575 Hydrogen bonding
318 ASP 2.91 3160 5565 Hydrogen bonding
318 ASP 1.91 5565 3167 Hydrogen bonding
366 GLU 3.17 3679 5585 Hydrogen bonding
366 GLU 2.84 5579 3674 Hydrogen bonding
PC-44215930 242 ASN 1.98 2430 5581 Hydrogen bonding
316 GLY 2.07 5583 3149 Hydrogen bonding
318 ASP 2.64 5558 3167 Hydrogen bonding
367 ASN 1.81 5582 3688 Hydrogen bonding

An AA indicates amino acid and a dash (–) indicates no interaction of specific atom

(b) Image showing the interacting amino acid residues in 2D conformation for Pc-44215930

graphic file with name 13205_2023_3677_Figi_HTML.jpg