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. 2013 Oct 22;8(10):e77558. doi: 10.1371/journal.pone.0077558

Figure 2. Structural comparison of OASS-A and OASS-B.

Figure 2

Panel A: Structure-based amino acid sequence alignment of OASS-A and OASS-B from Salmonella typhimurium. The alignment, carried out on the PDB entries 1OAS and 2JC3 using the Flexible structure AlignmenT (FATCAT) method [122], gave an overall identity of 40.32% and a similarity of 56.51%. Identical residues have a red background and residues with similar physicochemical properties are shown in red. Similarity scores were calculated by the ESPript program [123] using the Blosum62 matrix set at global score of 0.2. Residues of the first active site shell are indicated by dark circles below the alignment. Panel B: Active site of OASS-A. Residues of the first active site shell and PLP are shown in ball and stick style, colored pink and yellow, respectively. Panel C: Active site of OASS-B. Residues of the first active site shell and PLP are shown in ball and stick style, colored cyan and yellow, respectively.