 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](kw5005fig1mag.jpg)
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Figure 1
Protein-sequence alignment of the three manganese superoxide dismutases MnSOD-2 (SOD-2), MnSOD-3 (SOD-3) and human MnSOD (Borgstahl et al., 1992  ) with the secondary-structure elements of MnSOD-2 superposed. The two domains extend between residues 1 and 81 (N-domain), forming an α-hairpin with a turn between α2 and α3, and residues 90 and 197 (C-domain). Helix α7 is absent in MnSOD-3 owing to the deletion of residues 147–149. The alignment figure was made using the program ESPript (Gouet et al., 1999). Red boxes indicate strictly conserved residues. The helices labelled η1 and η2 represent 310-helix segments. Residues that are ligands to the manganese are boxed in blue. |
![[Figure 1]](kw5005fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
