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. Author manuscript; available in PMC: 2019 Oct 15.
Published in final edited form as: Arch Biochem Biophys. 2018 Aug 27;656:31–37. doi: 10.1016/j.abb.2018.08.012

Figure 2.

Figure 2.

The potential pY-pocket of SHIP2-SH2. (A) Cartoon representation of SHIP2-SH2 structure with conservative level for each residue analyzed using the ConSurf Server. Residue colors represent the conservative levels, ranging from cyan (variable) to purple (conserved). Twelve most conservative residues (conservative level 9) are labeled. ConSurf analysis was performed using the first structure of SHIP2-SH2 (PDB ID 2MK2) as a query for homologue search with search algorithm of HMMER. 150 homologous sequences were collected from UNIREF90 database for conservation score calculation with an E-value cut-off of 0.0001, maximal and minimal sequence identity of 95% and 35%, and HMMER iteration number of 1. (B) Molecular surface representation of SHIP2-SH2 structure (same orientation as in A) with conservative level for each residue. Only the most conservative residues on protein surface are labeled. (C) Molecular surface representation of SHIP2-SH2 structure with surface electrostatic potential analysis. Positively-charged residues around the potential pY-pocket are indicated.