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. 2017 Sep 13;18(Suppl 10):403. doi: 10.1186/s12859-017-1789-3

Fig. 3.

Fig. 3

Interactions module. The displayed data are from wild type protein p53 (1TSR.A) and its variants were selected using 70% identity and the PSI-BLAST alignment method. a All residues that establish hydrophobic interactions are colored in rose. The alignment position 50, which corresponds to mutation Val143Ala, was highlighted. b Hydrophobic interactions for mutation Val143Ala. The alignment position (column) 50 was selected to show only its hydrophobic interactions. The zoom of 30% was used to display short and long distance interactions. c 3D molecular representation of interactions for Val143 from protein p53 (1TSR.A). d Graphs (2D schematic representation) of p53 (1TSR.A) interactions for residue Val143