Skip to main content
Organic and Medicinal Chemistry Letters

Table 4 Human NADH-cytochrome b5 reductase protein residues interact with selected polyphenols, NADPH, beta-NADH using Glide docking simulation software (highlighted residues are H-bonding interacting residues) and FAD from X-ray Crystallized data of protein data bank

From: Plant polyphenols as electron donors for erythrocyte plasma membrane redox system: validation through in silico approach

S. No. ligands Interacting residues of receptor Human NADH-cytochrome b5 reductase No. of H-bond interaction
1. FAD Arg91, Pro92, Tyr93, Thr94, Val108, Ile109, Lys110, Phe113, Phe120, Gly123, Gly124, Lys125, Met126, Ser127, Gly179, Gly180, Thr181, Thr184 17
2. NADPH Thr94, Lys110, Try112, His117, Gly179, Gly180, Thr181, Thr184, Gln210, Cys273, Pro275 8
3. beta-NADH Tyr93, Lys110, Tyr112, Gly179, Gly180, Thr181, Gln210, Asp239, Phe251, Val252, Pro275 8
4. EGCG His117, Asn209, Gln210, Asp239, Phe251, Met278 4
5. Catechin Lys110, Tyr112, Gly180, Ala208, Asn209, Gln210, Phe251, Val252, Pro275 6
6. Quarcetin Lys110, Tyr112, Ala208, Asn209, Asp239, Phe251 4
7. Epicatechin Lys110, Tyr112, Gly180, Ala208, Gln210, Asp239, Phe251, Val252, Pro275 7
8. Reserveratrol Lys110, Tyr112, Ala208, Gln210, Phe251, Val252 3
Back to article page