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Identification
NameSuperoxide dismutase [Cu-Zn]
SynonymsNot Available
Gene NameSOD1
Enzyme Class
Biological Properties
General FunctionInvolved in metal ion binding
Specific FunctionDestroys radicals which are normally produced within the cells and which are toxic to biological systems
Cellular LocationCytoplasm. Mitochondrion intermembrane space.
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00372SuperoxideShow
YMDB00862hydronShow
YMDB00888Hydrogen peroxideShow
YMDB00900oxygenShow
GO Classification
Component
Not Available
Function
binding
ion binding
cation binding
metal ion binding
Process
metabolic process
cellular metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
superoxide metabolic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJR104C
Gene Sequence>465 bp ATGGTTCAAGCAGTCGCAGTGTTAAAGGGTGATGCCGGTGTCTCTGGTGTTGTCAAGTTC GAACAGGCTTCCGAATCCGAGCCAACCACTGTCTCTTACGAGATCGCTGGTAACAGTCCT AACGCAGAACGTGGGTTCCACATTCATGAGTTTGGAGATGCCACCAATGGTTGTGTCTCT GCTGGTCCTCACTTCAATCCTTTCAAGAAGACACATGGTGCTCCAACTGACGAAGTCAGA CATGTCGGTGACATGGGTAACGTAAAGACGGACGAAAATGGTGTGGCCAAGGGCTCCTTC AAGGACTCTTTGATCAAGCTTATCGGTCCTACCTCCGTTGTAGGCAGAAGCGTCGTTATC CACGCCGGCCAAGATGACTTAGGTAAGGGTGACACTGAAGAATCTTTGAAGACTGGTAAT GCCGGTCCAAGACCAGCCTGTGGTGTCATTGGTCTAACCAACTAA
Protein Properties
Pfam Domain Function
Protein Residues154
Protein Molecular Weight15854.59961
Protein Theoretical pI5.91
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Superoxide dismutase [Cu-Zn] MVQAVAVLKGDAGVSGVVKFEQASESEPTTVSYEIAGNSPNAERGFHIHEFGDATNGCVS AGPHFNPFKKTHGAPTDEVRHVGDMGNVKTDENGVAKGSFKDSLIKLIGPTSVVGRSVVI HAGQDDLGKGDTEESLKTGNAGPRPACGVIGLTN
References
External Links
ResourceLink
Saccharomyces Genome Database SOD1
Uniprot IDP00445
Uniprot NameSODC_YEAST
GenBank Gene IDAY558073
Genebank Protein ID45270036
PDB ID
1F1G
General Reference
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  • Djinovic, K., Gatti, G., Coda, A., Antolini, L., Pelosi, G., Desideri, A., Falconi, M., Marmocchi, F., Rolilio, G., Bolognesi, M. (1991). "Structure solution and molecular dynamics refinement of the yeast Cu,Zn enzyme superoxide dismutase." Acta Crystallogr B 47 ( Pt 6):918-927.1772629
  • Djinovic, K., Gatti, G., Coda, A., Antolini, L., Pelosi, G., Desideri, A., Falconi, M., Marmocchi, F., Rotilio, G., Bolognesi, M. (1992). "Crystal structure of yeast Cu,Zn superoxide dismutase. Crystallographic refinement at 2.5 A resolution." J Mol Biol 225:791-809.1602482
  • Ogihara, N. L., Parge, H. E., Hart, P. J., Weiss, M. S., Goto, J. J., Crane, B. R., Tsang, J., Slater, K., Roe, J. A., Valentine, J. S., Eisenberg, D., Tainer, J. A. (1996). "Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase." Biochemistry 35:2316-2321.8652572
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