Predicted structural organization of the p53 and Δp53 core domains illustrated by three-dimensional models. Illustrated are CPH predicted models  of the p53 and Δp53 isoforms using the RasMol program. The p53 core domain of 204 aa (total length of wild-type p53 is 393 aa) is predicted from aa 94 to 297 with a prediction identity of 100% (557.0 bits score) and the Δp53 core domain is predicted from aa 94 to 274 (total length of Δp53 is 327 aa) with a 93.4% identity and 451.5 bits score (protein position 274 in the Δp53 accordingly corresponds to protein position 340 in the full-length p53). Models and prediction structures for p53 (A) and Δp53 (B) are shown, and the variations are colored by secondary structures as follows: alpha helices in magenta, beta sheets in yellow, turns in pale blue, and all other residues are colored white. Differences between the isoform predictions are indicated with arrows and the N-terminal starting and C-terminal end points are marked in the figure. Due to the alternative splicing a major alpha-helical structure is missing in Δp53 (in A red arrow) and the tertiary protein structure of Δp53 is slightly more compact, as can bee seen from the moved alpha helix, indicated by green arrows. Below: uploaded protein core for the three-dimensional structure prediction query and received structural template.