Structures of a phosphosite from the disallowed and allowed region of conformation. A) Phosphorylation site in Catalase, a homo tetramer (PDB ID: 1QQW) is buried at interface and has a calculated rSASA of 0.18. We extracted the monomeric form of this protein and recalculated the rSASA value which is now 0.47 indicating that the site is now accessible. B) Protein Tyrosine-protein phosphatase has two conformations in which the phosphorylation site is buried in an auto inhibited (PDB ID: 2B3O) conformation with a rSASA value of 0.19 and it is accessible to the solvent (rSASA of 0.39) in an open conformation (PDB ID: 3PS5). C) Two structures of Mitogen-activated protein kinase 1 are aligned where the phosphosite is present adjacent to a segment which is ordered in one PDB and is disordered (PDBID: 2E14) in another conformation. The disordered segment lacks coordinates for the overhanging loop. The phosphosite has greater rSASA (0.35) in the structure with the disordered segment than in the ordered structure (0.16). D) Two different conformations of Voltage-dependent anion-selective channel protein 1 in which the local structural changes were observed at the site of phosphorylation. In PDBID: 2JK4 phosphorylation site is buried inside channel (rSASA 0.13) whereas in PDBID: 2K4T phosphorylation the site is oriented outside (rSASA of 0.52). E) In Mitogen-activated protein kinase 3, the phosphosite is near to activation loop (rSASA 0.19). F) The phosphosite in Eukaryotic initiation factor has a known consensus pattern of S/T-P-X-K/R (rSASA 0.11) for Cyclin dependent kinase. The octapeptide is shown in ball and stick representation. In Figures A, B, C, D, E phosphosite is shown in ball and sphere notation and the phosphorylated residue is colored in black.