Superoxide Dismutase

This page shows some interactive JSmol views of superoxide dismutases.

[CuZnSOD 1] shows the dimeric structure of one subunit of human Cu,Zn superoxide dismutase metalloprotein in the oxidised (Cu^II, Zn^II) form.

The protein chains are shown as cartoons to emphasise the secondary structure. The copper ion is shown as a green sphere and the zinc ion is shown as a blue/grey sphere.

[CuZnSOD 2] zooms in on the active site. Note the ligation and coordination geometry about the two metal ions, particularly the bridging histidine residue. Note also that the protein chain prevents access to the "back" of the copper ion - i.e. the sixth coordination site is blocked - there is only one amino acid between two coordinating His residues.

[CuZnSOD 3] is taken from the structure of the reduced (Cu^I, Zn^II) form of bovine CuZnSOD. Note that the His bridge has been lost and that the copper coordination number has changed.

Finally, [CuZnSOD 4] shows the "funnel" leading from the surface to the protein to the copper at the active site. Note the H-bonded water molecules in the "space" and the site of the conserved Arg residue.

[MnSOD 1] shows the structure of a manganese-containing superoxide dismutase from human mitochondria, this is a monomeric unit containing one manganese ion. In the close-up view, [MnSOD 2], note the coordination and geometry at the manganese (here in the reduced Mn^II form).