Table 2.
Interaction of SMC compounds with p53.
| Compound ID | Hydrophobic interactions | Hydrogen bonding | Cation-Pi interactions | Other residues involved | Binding energy (ΔG), kcal/mol | Binding affinity, Kd (M−1) |
|---|---|---|---|---|---|---|
| Site I | ||||||
| SMC-1 | – | Cys229, Thr231 | – | Gln144, Val197, Glu198, Gly199, Asn200, Val218, Pro219, Tyr220, Glu221, Glu224, Ser227, Thr230, Ile232, His233 | −6.186 | 3.44 × 104 |
| SMC-2 | – | Glu198, Gly199#, Asn200, His233 | – | Val197, Val218, Glu221, Pro222, Pro223, Glu224, Ser227, Cys229, Thr230, Thr231, Ile232 | −6.529 | 6.15 × 104 |
| SMC-3 | – | Asn200, Pro222, His233 | – | Val197, Glu198, Gly199, Val218, Glu221, Pro223, Glu224, Ser227, Cys229, Thr230, Thr231, Ile232 | −6.887 | 1.12 × 105 |
| SMC-4 | – | Thr231 | – | Gln144, Ile145, Val157, Val197, Glu198, Gly199, Asn200, Val218, Pro219, Tyr220, Glu221, Pro223, Glu224, Ser227, Cys229, Thr230, Ile232, His233 | −5.608 | 1.29 × 104 |
| SMC-5 | – | Glu198 | – | Val197, Gly199, Asn200, Val218, Pro219, Tyr220, Glu221, Thr230, Thr231, Ile232, His233 | −5.698 | 1.51 × 104 |
| Site II | ||||||
| SMC-1 | – | Val97, Ser99 | – | Ser96, Pro98, Arg158, Met160, Ile254, Thr256, Glu258, Arg267 | −5.106 | 5.56 × 103 |
| SMC-2 | – | Glu258, Gly262#, Arg267 | – | Ser96, Val97, Pro98, Ser99, Leu206, Asp208, Thr211, Arg213, Arg158, Met160, Ile254, Thr256, Asn263, Leu264 | −5.598 | 1.28 × 104 |
| SMC-3 | – | Ser99, Glu258 | Arg158 | Pro98, Met160, Arg213, Thr211, Asp208, Ile254, Thr256, Gly262, Leu264, Arg267 | −6.010 | 2.56 × 104 |
| SMC-4 | – | – | – | Ser96, Val97, Pro98, Ser99, Asp208, Arg209, Asn210, Thr211, Arg158, Met160, Ile254, Thr256, Glu258, Leu264, Arg267 | −5.711 | 1.54 × 104 |
| SMC-5 | – | Gly262, Arg267 | – | Pro98, Ser99, Arg158, Met160, Ile254, Thr256, Glu258, Asn263, Leu264 | −5.793 | 1.77 × 104 |
* Salt bridge.
#
Two bonds.