Fig. 6: Structural comparisons of nSMases.
From: Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
a Overall structural comparison of monomeric hSMPD2 (cyan), hSMPD3 (PDB code 5UVG; orange) and CODE (alpha fold predicted; purple). The TMHs from Isc1p adopt a 10-degree shift deviation compared with that of hSMPD2. b Structural comparison of monomeric hSMPD2 (cyan) and Isc1p (alpha fold predicted; purple). The black labeled and red labeled residues indicates the conserved and variable residues within the binding pocket. c Structural comparison of monomeric hSMPD2 (cyan) and hSMPD3 (PDB code 5UVG; orange). The black label indicates the conserved residues between SMPD2 and SMPD3. The red and orange labels indicate the variable residues in hSMPD2 and hSMPD3, respectively. d Surface representation of the substrate binding groove in Isc1p (purple). e Surface representation of the substrate binding groove in hSMPD2 (cyan). f Surface representation of the obstructed substrate binding groove in hSMPD3 (orange).
