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. Author manuscript; available in PMC: 2012 Feb 1.
Published in final edited form as: Proteins. 2011 Feb;79(2):417–427. doi: 10.1002/prot.22892

Figure 1. WT SOD1 and Mutation Sites.

Figure 1

SOD1 contains 153 residues and is biologically active in a homodimer form shown here, with each monomer containing a copper and zinc binding site. The bulk of the structure is a compact β-barrel and backs the active site. The residues associated with the mutations listed in Table 1, are shown with balls and sticks. Mutations with crystal structures are colored red and those that are computationally generated are colored yellow. The copper and zinc atoms are shown as dotted spheres. (Image prepared with PyMOL [33].)