Skip to main content
Fig. 3 | Journal of Biological Research-Thessaloniki

Fig. 3

From: Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi-1, the first member of a new bacterial lipase family (XVIII)

Fig. 3

Structural depiction of LipSm. a Superimposition of 3D-structures of CALA (turquoise) and LipSm (brown) indicating their catalytic triads (S154, D299, H330; LipSm numbering) and highlighting both their lid domains, with green and red colors for CALA and LipSm, respectively, whereas in purple is shown the additional active-site flap of CALA (E426 up to E436) that LipSm lacks. b ES complex of LipSm with the substrate butyl-butyrate, where are illustrated the catalytic triad of LipSm, and its conserved residues Q155 and Y211, which form the Y-type oxyanion hole of LipSm. The hydrogen bonds are illustrated as purple dotted lines

Back to article page