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TitleDisease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability
Journal, issue, pagesJ. Biol. Chem., Vol. 282, Page 345-352, Year 2007
Publish dateOct 24, 2006 (structure data deposition date)
AuthorsWang, J. / Caruano-Yzermans, A. / Rodriguez, A. / Scheurmann, J.P. / Slunt, H.H. / Cao, X. / Gitlin, J. / Hart, P.J. / Borchelt, D.R.
External linksJ. Biol. Chem. / PubMed:17092942
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-2nnx:
Crystal Structure of the H46R, H48Q double mutant of human [Cu-Zn] Superoxide Dismutase
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / Oxidoreductase; human; Cu-Zn superoxide dismutase; superoxide acceptor; familial amyotrophic lateral sclerosis mutant

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