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Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)

 SODC_YEAST              Reviewed;         154 AA.
P00445; D6VWS3; Q68HB2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 210.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
Name=SOD1; OrderedLocusNames=YJR104C; ORFNames=J1968;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3290902; DOI=10.1073/pnas.85.13.4789;
Bermingham-Mcdonogh O., Gralla E., Valentine J.;
"The copper, zinc-superoxide dismutase gene of Saccharomyces
cerevisiae: cloning, sequencing, and biological activity.";
Proc. Natl. Acad. Sci. U.S.A. 85:4789-4793(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Ping Y.;
"Cloning and sequence analysis of copper, zinc-superoxide dismutase
gene.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
PROTEIN SEQUENCE OF 2-154.
Johansen J.T., Overballe-Petersen C., Martin B., Hasemann V.,
Svendsen I.;
"The complete amino acid sequence of copper, zinc superoxide dismutase
from Saccharomyces cerevisiae.";
Carlsberg Res. Commun. 44:201-217(1979).
[7]
PROTEIN SEQUENCE OF 2-154.
PubMed=6993479;
Steinman H.M.;
"The amino acid sequence of copper-zinc superoxide dismutase from
bakers' yeast.";
J. Biol. Chem. 255:6758-6765(1980).
[8]
PROTEIN SEQUENCE OF 2-11.
STRAIN=ATCC 26786 / X2180-1A;
Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[9]
SUBCELLULAR LOCATION.
PubMed=11500508; DOI=10.1074/jbc.M105296200;
Sturtz L.A., Diekert K., Jensen L.T., Lill R., Culotta V.C.;
"A fraction of yeast Cu,Zn-superoxide dismutase and its
metallochaperone, CCS, localize to the intermembrane space of
mitochondria. A physiological role for SOD1 in guarding against
mitochondrial oxidative damage.";
J. Biol. Chem. 276:38084-38089(2001).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-70, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15166219; DOI=10.1074/jbc.M404173200;
Zhou W., Ryan J.J., Zhou H.;
"Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
Induction of protein sumoylation by cellular stresses.";
J. Biol. Chem. 279:32262-32268(2004).
[12]
MUTAGENESIS OF GLY-123; 131-ASP-THR-132; PRO-143 AND PRO-145.
PubMed=15069187; DOI=10.1073/pnas.0308298101;
Carroll M.C., Girouard J.B., Ulloa J.L., Subramaniam J.R., Wong P.C.,
Valentine J.S., Culotta V.C.;
"Mechanisms for activating Cu- and Zn-containing superoxide dismutase
in the absence of the CCS Cu chaperone.";
Proc. Natl. Acad. Sci. U.S.A. 101:5964-5969(2004).
[13]
MUTAGENESIS OF PRO-143 AND PRO-145.
PubMed=16234242; DOI=10.1074/jbc.M509142200;
Jensen L.T., Culotta V.C.;
"Activation of CuZn superoxide dismutases from Caenorhabditis elegans
does not require the copper chaperone CCS.";
J. Biol. Chem. 280:41373-41379(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-117 AND THR-132,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-39 AND SER-99,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-99 AND THR-138,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=22984289; DOI=10.1074/mcp.M112.021105;
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
"Intermembrane space proteome of yeast mitochondria.";
Mol. Cell. Proteomics 11:1840-1852(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1772629; DOI=10.1107/S0108768191004949;
Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A.,
Falconi M., Marmocchi F., Rotilio G., Bolognesi M.;
"Structure solution and molecular dynamics refinement of the yeast
Cu,Zn enzyme superoxide dismutase.";
Acta Crystallogr. B 47:918-927(1991).
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1602482; DOI=10.1016/0022-2836(92)90401-5;
Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A.,
Falconi M., Marmocchi F., Rotilio G., Bolognesi M.;
"Crystal structure of yeast Cu,Zn superoxide dismutase.
Crystallographic refinement at 2.5-A resolution.";
J. Mol. Biol. 225:791-809(1992).
[21]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
IONS.
PubMed=8652572; DOI=10.1021/bi951930b;
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.;
"Unusual trigonal-planar copper configuration revealed in the atomic
structure of yeast copper-zinc superoxide dismutase.";
Biochemistry 35:2316-2321(1996).
[22]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG; COPPER AND ZINC, AND DISULFIDE BONDS.
PubMed=10026301; DOI=10.1021/bi982284u;
Hart P.J., Balbirnie M.M., Ogihara N.L., Nersissian A.M., Weiss M.S.,
Valentine J.S., Eisenberg D.;
"A structure-based mechanism for copper-zinc superoxide dismutase.";
Biochemistry 38:2167-2178(1999).
[23]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ZINC AND CCS1,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=11524675; DOI=10.1038/nsb0901-751;
Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C.;
"Heterodimeric structure of superoxide dismutase in complex with its
metallochaperone.";
Nat. Struct. Biol. 8:751-755(2001).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 1 copper ion per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Homodimer in holo form. In apo form, heterodimer with
CCS1. Zinc-binding at 'His-16' of CCS1 and Glu-43 of apo-SOD1 is
required for this heterodimerization.
{ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675,
ECO:0000269|PubMed:8652572}.
-!- INTERACTION:
P40202:CCS1; NbExp=5; IntAct=EBI-17635, EBI-10287;
P06787:CMD1; NbExp=2; IntAct=EBI-17635, EBI-3976;
P16474:KAR2; NbExp=2; IntAct=EBI-17635, EBI-7876;
P23291:YCK1; NbExp=2; IntAct=EBI-17635, EBI-4718;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11500508}.
Mitochondrion intermembrane space {ECO:0000269|PubMed:11500508,
ECO:0000269|PubMed:22984289}. Note=A small percentage (around 1-5
percent) localizes to the mitochondrial intermembrane space.
-!- MISCELLANEOUS: Present with 519000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
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EMBL; J03279; AAA34543.1; -; Genomic_DNA.
EMBL; AY690619; AAT99430.1; -; Genomic_DNA.
EMBL; Z49604; CAA89634.1; -; Genomic_DNA.
EMBL; AY558073; AAS56399.1; -; Genomic_DNA.
EMBL; BK006943; DAA08889.1; -; Genomic_DNA.
PIR; A36171; DSBYC.
RefSeq; NP_012638.1; NM_001181762.1.
PDB; 1B4L; X-ray; 1.80 A; A=2-154.
PDB; 1B4T; X-ray; 1.80 A; A=2-154.
PDB; 1F18; X-ray; 1.70 A; A=1-154.
PDB; 1F1A; X-ray; 1.80 A; A=1-154.
PDB; 1F1D; X-ray; 2.10 A; A=1-154.
PDB; 1F1G; X-ray; 1.35 A; A/B/C/D/E/F=1-154.
PDB; 1JCV; X-ray; 1.55 A; A=2-154.
PDB; 1JK9; X-ray; 2.90 A; A/C=2-154.
PDB; 1SDY; X-ray; 2.50 A; A/B/C/D=2-154.
PDB; 1YAZ; X-ray; 1.70 A; A=2-154.
PDB; 1YSO; X-ray; 1.73 A; A=2-154.
PDB; 2JCW; X-ray; 1.70 A; A=2-154.
PDBsum; 1B4L; -.
PDBsum; 1B4T; -.
PDBsum; 1F18; -.
PDBsum; 1F1A; -.
PDBsum; 1F1D; -.
PDBsum; 1F1G; -.
PDBsum; 1JCV; -.
PDBsum; 1JK9; -.
PDBsum; 1SDY; -.
PDBsum; 1YAZ; -.
PDBsum; 1YSO; -.
PDBsum; 2JCW; -.
ProteinModelPortal; P00445; -.
SMR; P00445; -.
BioGrid; 33860; 243.
ComplexPortal; CPX-2267; SOD1-CCS1 Superoxide Dismutase heterodimer.
ComplexPortal; CPX-2896; [Cu-Zn] Superoxide dismutase complex.
DIP; DIP-5859N; -.
IntAct; P00445; 17.
MINT; P00445; -.
STRING; 4932.YJR104C; -.
MoonProt; P00445; -.
iPTMnet; P00445; -.
SWISS-2DPAGE; P00445; -.
MaxQB; P00445; -.
PaxDb; P00445; -.
PRIDE; P00445; -.
TopDownProteomics; P00445; -.
EnsemblFungi; YJR104C; YJR104C; YJR104C.
GeneID; 853568; -.
KEGG; sce:YJR104C; -.
EuPathDB; FungiDB:YJR104C; -.
SGD; S000003865; SOD1.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
InParanoid; P00445; -.
KO; K04565; -.
OMA; IHTFGDN; -.
OrthoDB; EOG092C578I; -.
BioCyc; YEAST:MONOMER3O-1629; -.
Reactome; R-SCE-114608; Platelet degranulation.
Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
EvolutionaryTrace; P00445; -.
PRO; PR:P00445; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0004784; F:superoxide dismutase activity; IDA:SGD.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IMP:SGD.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:SGD.
GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
GO; GO:1901856; P:negative regulation of cellular respiration; IMP:SGD.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IMP:SGD.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:SGD.
GO; GO:0050821; P:protein stabilization; IMP:SGD.
GO; GO:0006801; P:superoxide metabolic process; IMP:SGD.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Copper; Cytoplasm;
Direct protein sequencing; Disulfide bond; Isopeptide bond;
Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
Reference proteome; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6993479,
ECO:0000269|Ref.6, ECO:0000269|Ref.8}.
CHAIN 2 154 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164129.
METAL 43 43 Zinc 2; shared with CCS1; in apo form.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:11524675}.
METAL 47 47 Copper; catalytic.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:8652572}.
METAL 49 49 Copper; catalytic.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:8652572}.
METAL 64 64 Copper; catalytic.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:8652572}.
METAL 64 64 Zinc 1; structural.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:11524675}.
METAL 72 72 Zinc 1; structural.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:11524675}.
METAL 81 81 Zinc 1; structural.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:11524675}.
METAL 84 84 Zinc 1; structural.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:11524675}.
METAL 121 121 Copper; catalytic.
{ECO:0000269|PubMed:10026301,
ECO:0000269|PubMed:8652572}.
BINDING 144 144 Substrate. {ECO:0000305}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 132 132 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 138 138 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
DISULFID 58 147
DISULFID 58 58 Interchain (with C-229 in CCS1); in
linked form.
CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15166219}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15166219}.
MUTAGEN 123 123 G->K: Does not enable copper chaperone-
independent activation.
{ECO:0000269|PubMed:15069187}.
MUTAGEN 131 132 DT->GN: Does not enable copper chaperone-
independent activation.
{ECO:0000269|PubMed:15069187}.
MUTAGEN 143 143 P->A,S: Enables copper chaperone-
independent activation; when associated
with A-145 or with L-145.
{ECO:0000269|PubMed:15069187,
ECO:0000269|PubMed:16234242}.
MUTAGEN 145 145 P->A,L: Enables copper chaperone-
independent activation; when associated
with A-143 or with S-143.
{ECO:0000269|PubMed:15069187,
ECO:0000269|PubMed:16234242}.
CONFLICT 56 56 N -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 93 93 N -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
STRAND 3 9 {ECO:0000244|PDB:1F1G}.
STRAND 11 13 {ECO:0000244|PDB:1F1G}.
STRAND 15 21 {ECO:0000244|PDB:1F1G}.
STRAND 23 27 {ECO:0000244|PDB:1SDY}.
STRAND 29 37 {ECO:0000244|PDB:1F1G}.
STRAND 43 50 {ECO:0000244|PDB:1F1G}.
TURN 55 58 {ECO:0000244|PDB:1F1G}.
HELIX 59 61 {ECO:0000244|PDB:1F1G}.
STRAND 77 80 {ECO:0000244|PDB:1F1G}.
STRAND 84 89 {ECO:0000244|PDB:1F1G}.
STRAND 96 104 {ECO:0000244|PDB:1F1G}.
STRAND 107 109 {ECO:0000244|PDB:1F1G}.
STRAND 116 120 {ECO:0000244|PDB:1F1G}.
STRAND 130 132 {ECO:0000244|PDB:1F1G}.
HELIX 135 138 {ECO:0000244|PDB:1F1G}.
STRAND 146 149 {ECO:0000244|PDB:1F1G}.
STRAND 151 153 {ECO:0000244|PDB:1F1G}.
SEQUENCE 154 AA; 15855 MW; E263A74679AF11F7 CRC64;
MVQAVAVLKG DAGVSGVVKF EQASESEPTT VSYEIAGNSP NAERGFHIHE FGDATNGCVS
AGPHFNPFKK THGAPTDEVR HVGDMGNVKT DENGVAKGSF KDSLIKLIGP TSVVGRSVVI
HAGQDDLGKG DTEESLKTGN AGPRPACGVI GLTN


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LF-MA0065 anti-Superoxide Dismutase 2 (4F10) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0019 anti-Superoxide Dismutase 4 (11G1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0023 anti-Superoxide Dismutase 1 (72B1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-MA0121 anti-Superoxide Dismutase 3 (1H12), Mouse monoclonal to Superoxide Dismutase 3, Isotype IgG2b, Host Mouse 100 ul
LF-MA0066 anti-Superoxide Dismutase 2 (23G5) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
SCH-MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
LF-MA0030 anti-Superoxide Dismutase 2 (2A1), Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0035 anti-Superoxide Dismutase 2 (1E8) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG2b, Host Mouse 100 ul
LF-MA0016 anti-Superoxide Dismutase 4 (2A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0042 anti-Superoxide Dismutase 4 (3A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG2a, Host Mouse 100 ul
LF-MA0029 anti-Superoxide Dismutase 1 (8A1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-PA10015 anti-Superoxide Dismutase 2, Mouse polyclonal to Superoxide Dismutase 2, Isotype , Host Mouse 50 ug
LF-PA0021 anti-Superoxide Dismutase 2, Rabbit polyclonal to Superoxide Dismutase 2, Isotype IgG, Host Rabbit 100 ul
LF-PA0013 anti-Superoxide Dismutase 1, Rabbit polyclonal to Superoxide Dismutase 1, Isotype IgG, Host Rabbit 100 ul
orb80178 Human Superoxide Dismutase (homodimer) protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is homodimer, non-glycosylated polypeptide chain containing 2x 154 amino acids and having 100
8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU
SCH-8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU


 

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