DSSP-web

DSSP-web is a tool to assign the secondary structure in a protein by DSSP program [Kabsch and Sander, 1983] based on the analysis of backbone dihedral angles and hydrogen bonds. DSSP assigns seven different secondary structures, i.e., H: a-helix, G: 310 helix, I: p-helix, E: extended strand, B: residue in isolated b-bridge, S: bend, and T: H-bonded turn. In addition, a ‘‘coil’’ state is assigned when no secondary structure is recognized.

The user can indicate the protein name, paste the file PDB in the box and choose three possible analysing options.
In the first analysis option DSSP-web shows the file obtained by DSSP program.
In the results page of the second option DSSP-web shows the sequence and secondary structure of the analysed protein reporting on each line 50 residues with an empty space between blocks of 10. The helices and beta-strands are evidenced in red and yellow, respectively example1.
When the user chooses the third option, DSSP-web reports the table with the different secondary structures and the percentage of residues present in each of these example2.

Click here to access the input form.