Table 4 Interaction sites, bond sites and bond distance, between collagen (Type I) and four ligands.
From: Bioinformatics in crosslinking chemistry of collagen with selective cross linkers
Ligand | Interaction sites | Bond | Bond distance in(A°) |
|---|---|---|---|
| Â | Collagen type-I | Â | Â |
Dopaquinone | Eleventh residue Val of C-chain (α2) | Val C 12(Cα)-O· · ·N(Dopaquinone) | 3.04 |
|  | Thirteenth residue Gly of C-chain (α2) | Gly C 13(Cα)-O· · ·H(Dopaquinone) | 2.26 |
|  | Fourteenth residue Pro of C-chain (α2) | Pro C 14(Cα)-CA· · ·O(Dopaquinone) | 3.07 |
|  | Seventh residue Asn of A-chain (α1) | Asn A 17(Cα)-N· · ·O(Dopaquinone) | 2.79 |
Potassium embelate | Eleventh residue Val of C-chain (α2) | Val C 12(Cα)-N· · ·O(Potassium embelate) | 3.03 |
|  | Eleventh residue Val of C-chain (α2) | Val C 12(Cα)-O· · ·O(Potassium embelate) | 3.38 |
Embelin | Eleventh residue Val of C-chain (α2) | Val C 12(Cα)-N· · ·O(Embelin) | 3.22 |
|  | Thirteenth residue Gly of C-chain (α2) | Gly C 13(Cα)-O· · ·H(Embelin) | 2.74 |
|  | Fourteenth residue Pro of C-chain (α2) | Pro C 14(Cα)-N· · ·O(Embelin) | 4.11 |
5-O-Methyl embelin | Eleventh residue Val of C-chain (α2) | Val C 12(Cα)-N· · ·O(5-O-Methyl embelin) | 3.16 |
|  | Fourteenth residue Pro of C-chain (α2) | Pro C 14(Cα)-N· · ·O(5-O-Methyl embelin) | 3.1 |
|  | Fifteenth residue Tyr of C-chain (α2) | Tyr C 15(Cα)-N· · ·O(5-O-Methyl embelin) | 3.23 |