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Figure 2 | BMC Structural Biology

Figure 2

From: Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors

Figure 2

An extract from all IFR positions showing the most restrictive ones, identified for four serine proteases subfamilies, bound to BPTI. The positions shown are among the most restrictive ones in terms of the type of residues occupying them in 4 sub families of serine proteases: trypsins; chymotrypsins; elastases and thrombins, respectively. Those residue types that are present in at least 50% or more of analyzed proteases within a single subfamily, at a given IFR position, are indicated by a '*' sign. The colors of residues correspond to STING AA color coding {see text for details as well as the legend for the Table 1}: green are P olar, gray are H ydrophobic, red are negatively C harged, blue (and cyan for His) are positively C harged residues. The gray background color is used to indicate those IFR positions which are populated, within a sub family, by a single residue type or are absent from the IFR ensemble (represented by "-"). Those IFR positions occupied in each of four sub families by one predominant class of amino acid (indicated by "*") are labeled in light gray.

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