Table 4. Change in Accessible surface area and binding interactions of the site I amino acid residues of HSA with uremic toxin creatinine.
Ligands | Amino acidresidue | ΔASA (Å2) | Location | Electrostatic Interaction | Number of other interacting residues (5 Å) | GOLD Fitness score | X-score |
Creatinine | Arg257Leu238Ala291Ser287Leu260 | 17.9617.0816.0512.0210.58 | IIa-h4IIa-h6IIa-h3IIa-h6IIa-h4 | Hydrogen bondC = O…H2NArg257(2.85 Å) | 10 | 28.16 | −5.68 |
Phenyl-butazone | Ala 291Leu238Leu242Trp214Arg257Ile264Arg222Leu219Ser287Ile290Leu260 | 42.941.7933.6622.6118.9513.0412.8212.6912.0211.4811.17 | IIa-h6IIa-h3IIa-h3IIa-h2IIa-h4IIa-h4IIa-h2IIa-h2IIa-h6IIa-h6IIa-h4 | 15 | 47.82 | −8.49 | |
Warfarin | Leu238Ala291Leu242Trp214Arg257Arg222Leu219Ser287Ile290Phe211Leu260 | 39.0338.635.628.9316.414.0512.2512.0211.4811.2610.72 | IIa-h3IIa-h6IIa-h3IIa-h2IIa-h4IIa-h2IIa-h2IIa-h6IIa-h6IIa-h2IIa-h4 | 15 | 41.62 | −8.05 |