Figure 2 | Scientific Reports

Figure 2

From: Crystal structure of Pelagibacterium halotolerans PE8: New insight into its substrate-binding pattern

Figure 2

Amino acid sequence alignment of PE8 (PDB: 5DWD) with homologs from the LPCE family. RspE, from R. sphaeroides (PDB: 4FHZ); PfEstII, esterase II from P. fluorescens (PDB: 1AUO); PA3859, from P. aeruginosa (PDB: 3CN9); FTT258, from F. tularensis (PDB: 4F21); APT1, from human (PDB: 1FJ2); LYPLAL1, from human (PDB: 3U0V). Identical and similar residues among groups are shown in white font on a red background and in red font on a white background, respectively. Triangles represent the locations of the catalytic active sites (serine (S), aspartate (D) and histidine (H)) and squares represent the residues located on the oxyanion hole (tyrosine (Y)/tryptophan (W)/valine (V)/leucine (L)/serine (S) and glutamine (Q)/methionine (M)). Black boxes represent the locations of residues Arg79 and Arg83 of PE8. The secondary structural elements α-helices, 310-helices and β-strands of PE8 are denoted by α, η and β, respectively, with symbols above the sequences.

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