Fig. 4: Comparison of ehSMOX with mPAOX structures.
From: Structure of human spermine oxidase in complex with a highly selective allosteric inhibitor
a Superimposition of the ribbon representation of ehSMOX (in blue) bound to MDL72527 (in orange sticks) and mPAOX (PDB: 5MBX in green) with its substrate N-AcSpm (in magenta sticks). FAD is depicted in yellow and green, respectively for ehSMOX and mPAOX and the ehSMOX cystine bridge (Cys187-Cys373) is shown in yellow sticks. b Residues involved in π-interactions are in light green sticks for mPAOX and in blue for heSMOX; the dashed line indicated the additional H-bond between E185 and Y123 only present in ehSMOX. c The Sα3 helix of mPAOX (transparent green ribbon) is longer compared to ehSMOX and directed towards the back of the protein. In ehSMOX, the cysteine bridge depicted in yellow sticks indicates the end of helix Sα3 and the beginning of the loop directed in the opposite direction compared to mPAOX. Residue S190 of heSMOX clashes with the N-AcSpm (in magenta stick) superimposed from mPAOX structure.
