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TitleInsights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.
Journal, issue, pagesJ. Biol. Chem., Vol. 290, Page 2405-2418, Year 2015
Publish dateAug 21, 2013 (structure data deposition date)
AuthorsSea, K. / Sohn, S.H. / Durazo, A. / Sheng, Y. / Shaw, B.F. / Cao, X. / Taylor, A.B. / Whitson, L.J. / Holloway, S.P. / Hart, P.J. ...Sea, K. / Sohn, S.H. / Durazo, A. / Sheng, Y. / Shaw, B.F. / Cao, X. / Taylor, A.B. / Whitson, L.J. / Holloway, S.P. / Hart, P.J. / Cabelli, D.E. / Gralla, E.B. / Valentine, J.S.
External linksJ. Biol. Chem. / PubMed:25433341
MethodsX-ray diffraction
Resolution2.2 - 2.6 Å
Structure data

PDB-4mcm:
Human SOD1 C57S Mutant, As-isolated
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-4mcn:
Human SOD1 C57S Mutant, Metal-free
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / HUMAN CU / ZN SUPEROXIDE DISMUTASE / ANTIOXIDANT / METAL-BINDING / AMYOTROPHIC LATERAL SCLEROSIS / DISULFIDE BOND

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