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Fig. 4 | Microbial Cell Factories

Fig. 4

From: Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium

Fig. 4

Active site of SfSFGH. a The substrate-binding site (yellow circle) of SfSFGH has a positively charged surface. b The conserved catalytic triad (Ser148, Asp24, and His257) residues are located on the substrate-binding site. The residues creating a substrate-binding site are presented as a stick model. c Dimerization of SfSFGH is mediated by the α2, α3, and α12 helices. The β1-strand also participates in the dimerization interaction

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