Table 5 Interaction sites, bond sites and bond distance, between collagen (Type III) 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-III | Â | Â |
Dopaquinone | Eleventh residue Val of B-chain (α1) | Val B 12(Cα)-O· · ·N(Dopaquinone) | 2.6 |
|  | Eleventh residue Val of B-chain (α1) | Val B 12(Cα)-O· · ·O(Dopaquinone) | 2.83 |
|  | Fourteenth residue Pro of B-chain (α1) | Pro B 14(Cα)-N· · ·O(Dopaquinone) | 2.97 |
|  | Fifteenth residue Ala of B-chain (α1) | Asn B 15(Cα)-N· · ·O(Dopaquinone) | 3.02 |
Embelin | Eleventh residue Lys of B-chain (α1) | Lys B 12(Cα)-N· · ·O(Embelin) | 3.02 |
|  | Thirteenth residue Gly of B-chain (α1) | Gly B 13(Cα)-O· · ·O(Embelin) | 2.72 |
Potassium embelate | Thirteenth residue Gly of B-chain (α1) | Gly B 13(Cα)-O· · ·O(Potassium embelate) | 2.62 |
|  | Fourteenth residue Pro of B-chain (α1) | Pro C 14(Cα)-N· · ·O(Potassium embelate) | 2.98 |
5-O-Methyl embelin | Eleventh residue Lys of C-chain (α1) | Lys C 12(Cα)-O· · ·O(5-O-Methyl embelin) | 2.72 |
|  | Fourteenth residue Pro of C-chain (α2) | Pro C 14(Cα)-O· · ·O(5-O-Methyl embelin) | 3.45 |