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4MCM

Human SOD1 C57S Mutant, As-isolated

Summary for 4MCM
Entry DOI10.2210/pdb4mcm/pdb
Related4MCN
DescriptorSuperoxide dismutase [Cu-Zn], ZINC ION, SULFATE ION, ... (4 entities in total)
Functional Keywordsoxidoreductase, human cu, zn superoxide dismutase, antioxidant, metal-binding, amyotrophic lateral sclerosis, disulfide bond
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P00441
Total number of polymer chains12
Total formula weight192652.65
Authors
Sea, K.,Sohn, S.H.,Durazo, A.,Sheng, Y.,Shaw, B.,Cao, X.,Taylor, A.B.,Whitson, L.J.,Holloway, S.P.,Hart, P.J.,Cabelli, D.E.,Gralla, E.B.,Valentine, J.S. (deposition date: 2013-08-21, release date: 2014-08-27, Last modification date: 2023-09-20)
Primary citationSea, 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.
Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.
J.Biol.Chem., 290:2405-2418, 2015
Cited by
PubMed: 25433341
DOI: 10.1074/jbc.M114.588798
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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