Bioinorganic Chemistry and Applications / 2018 / Article / Tab 6

Research Article

A Diversified Spectrometric and Molecular Docking Technique to Biophysical Study of Interaction between Bovine Serum Albumin and Sodium Salt of Risedronic Acid, a Bisphosphonate for Skeletal Disorders

Table 6

Type of interactions, involvement, and their distances between amino acids present in BSA after interaction with RSN for three binding sites by molecular docking studies.

Binding siteInteractionsAmino acid-RSN atom
TypeDistance (Å)

Site I (IIA)Conventional hydrogen bond2.10ARG:256:HE–N1
1.93ILE289:O–H7
2.16ARG217:HE–O7
van der WaalsSER286
ILE263
VAL292
Carbon hydrogen bond3.72LYS221:CE–O7
Unfavorable positive–positive5.24LYS221:NZ–P2
Pi–alkyl5.03LEU259:(CG–CD1–D2)–aromatic ring
5.31ILE289:(CB–CG1–CD1)–aromatic ring
4.95ARG256: (CB–CG)–aromatic ring

Site II (IIIA)Conventional hydrogen bond2.64ARG409:HE–O7
2.00ASN:OD1–H9
2.37ASN390:HD22–O7
2.80THR448:HG1–N1
2.24TYR410:HH–O6
1.97SER488:OG–H7
van der WaalsPHE402
LEU406
LEU429
LEU456
LEU386
ARG484
Unfavorable positive–positive3.33ARG409:P1–NH2
Pi–alkyl5.06LEU452:CG–aromatic ring

Site III (IB)Pi–sigma3.93VAL432:CG1–aromatic ring
Conventional hydrogen bond1.96TYR160:HH–O5
van der WaalsLYS136
PRO117
GLU140
Pi–sigma3.96LEU115:O1–aromatic ring