Table 1 Molecular docking shows the binding affinity of Polyphyllin B with ALB, TP53, EGFR, STAT3, and ESR1
Polyphyllin B | Binding energy (kcal/mol) | Interacting amino acid residues | ||
|---|---|---|---|---|
hydrogen bonds | hydrophobic interactions | Van der Waals forces | ||
ALB | -10.7 | A chain: GLN 390, GLU 393, GLN 397 B chain: ASP 375 ALA 371 VAL 310 | A chain: LYS 389 B chain: PHE 374 ALA 306 HIS 338 ARG 337 LEU 302 MET 298 | A chain: ASN 386 B chain: VAL 373 VAL 310 LYS 372 HIS 367 GLU 311 LEU 305 SER 304 ASP 301 ALA 300 |
TP53 | -9.1 | A chain: SER 166 GLN 100 B chain: ARG 196 GLU 198 | B chain: LEU 137 TYR 239 HIS 178 HIS 179 ALA 138 | A chain: MET 169 THR 102 LEU 252 LYS 164 LYS 101 B chain: ASN 235 ASP 184 ASP 186 THR 140 MET 237 GLY 199 MET 237 LYS 139 |
EGFR | -9.5 | A chain: ASP 800 MET 793 GLY 719 | A chain: ARG 841 LEU 718 | A chain: ASN 842 LEU 844 ALA 743 LEU 792 LEU 1001 GLY 796 LYS 745 PHE 997 VAL 726 SER 720 GLY 721 LYS 875 THR 725 PRO 794 TRP 880 ASP 916 GLY 917 LYS 879 LYS 913 |
STAT3 | -11.2 | A chain: TYR 446 GLU 357 HIS 447 | A chain: LYS 282 B chain: LEU 358 LYS 363 | A chain: GLU 286 GLN 289 GLY 449 GLN 448 LEU 358 B chain: VAL 393 TYR 446 TYR 360 GLN 361 GLN 448 GLY 449 TYR 360 GLU 357 |
ESR1 | -8.6 | A chain: LYS 362 PHE 367 LEU 308 LEU 310 ASP 369 | A chain: HIS 550 ALA 551 ARG 548 ALA 546 VAL 368 ARG 363 ALA 318 | HIS 547 ALA 322 VAL 364 SER 309 ALA 307 GLY 366 PRO 365 GLN 314 HIS 474 ALA 322 |