Nucleic Acids Research, 2012, Vol. 40, Web Server issue W215 protein graphs. After the comparison of the query pro- tein to every nr-PDB protein structure is complete, the degrees of structural conservation are calculated for all amino acid residues in the query protein. These are analogous to degrees of sequence conservation, repre- sented, e.g. in sequence logos with amino acid letters of different sizes, and reveal the frequency of occurrence of a particular residue in the local structural alignments that were found in the nr-PDB. These degrees of structural conservation are represented as different colors on the query protein structure as in Figure 3A, and often indicate the position of binding or other functionally important sites. The latest ProBiS web server shown in Figure 1 has a number of powerful features. It has an order of magnitude faster computation time, pre-calculated results and an improved user interface. All the functions of the ProBiS web server can now be accessed fully automatically from user scripts through the new ProBiS web services based on RESTful (Representational State Transfer) technology (30). The new additions to the ProBiS web server invite users to explore similarities among binding sites in Figure 1. ProBiS web server page provides access to the Protein Binding Sites Tools.