 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](dz5262fig3mag.jpg)
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Figure 3
Structural similarity to the cysteine protease superfamily. (a) Alignment of the catalytic triads from representative structural matches to SseI. Cys178, His216 and Asp231 of SseI are shown in red and the distances between these residues are given in Å. (b–e) Structural alignments of SseI (blue; catalytic triad in red) with (b) PMT (gray; PDB entry 2ec5 ; residues 1105–1285; triad Cys1165/His1205/Asp1220; Kitadokoro et al., 2007  ), (c) protein-glutaminase (magenta; PDB entry 2zk9
; residues 1–185; triad Cys42/His83/Asp103; Hashizume et al., 2011), (d) AvrPphB (green; PDB entry 1ukf
; residues 81–268; triad Cys98/His212/Asp227; Zhu et al., 2004), (e) sea bream transglutaminase (orange; PDB entry 1g0d
; residues 141–460; triad Cys272/His332/Asp355; Noguchi et al., 2001), (f) S. typhimurium NAT (yellow; PDB entry 1e2t
; residues 1–271; triad Cys69/His107/Asp122; Sinclair et al., 2000) and (g) yeast PNGase (brown; PDB entry 3esw
; residues 1–329; triad Cys191/His218/Asp235; Zhao et al., 2009). |
![[Figure 3]](dz5262fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
