Fig. 1
From: Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate
The structure of I. sakaiensis MHETase displays a bipartite domain architecture. a I. sakaiensis PETase and MHETase degrade PET to terephthalic acid and ethylene glycol. Side products are not shown. b MHETase structure with the α/β-hydrolase domain (MHETaseHyd) colored in salmon and the lid domain (MHETaselid) in light blue. Disulfide bonds are shown as sticks. c Close-up view of the MHETase catalytic triad, oxyanion hole and the water molecules in the substrate-binding site. d A. oryzae FaeB (PDB-ID: 3WMT24), α/β-hydrolase domain (AoFaeBHyd) in crimson red, lid domain (AoFaeBLid) in cyan. e Close-up view of the AoFaeB catalytic triad, oxyanion hole and the water molecules in the substrate-binding site. Dashed lines indicate hydrogen bonds, rotation angles relate to the overview. Interacting residues are shown as sticks and colored by atom type. Carbon—as given for the respective molecule; nitrogen—blue; oxygen—red; sulfur—yellow. Water oxygens are shown as green spheres. Calcium is shown as purple sphere
