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. 2022 Feb 3;54(1):495–506. doi: 10.1080/07853890.2022.2033826

Table 2.

Molecular docking details of isolated compounds 1 and 2 and against urease and tyrosinase enzymes.

Compound Hydrogen bonding residues and distance Hydrophobic interacting residues B. affinity (kcal/mol)
1 His541 3.32 Å His408, Cys442, Leu488, His491, Ile517 and Tyr543 –8.7
2 Ala439 2.69 Å Cys405, His408, Thr437, Cys442, Leu488, His491, Ile517, His541 and Tyr543 –8.7
Thiourea (standard)     –3.4
1 No H bonding Gly62, Phe90, Trp93, Val262, Phe292 and His296 –7.6
2 No H bonding Phe90, Val262, Phe292, His295 and His296 –7.5
Kojic acid (standard)     –5.1