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InterPro: IPR001424 Superoxide dismutase, copper/zinc binding

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1900 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR001424 SOD_Cu_Zn

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.40.200	SOD_Cu_Zn	1797
Pfam	PF00080	Sod_Cu	1786
PRINTS	PR00068	CUZNDISMTASE	957
PANTHER	PTHR10003	SOD_Cu_Zn	1761
SuperFamily	SSF49329	SOD_Cu_Zn	1869
Signatures in BioMart

InterPro Relationships Help

Contains

IPR018152 Superoxide dismutase, copper/zinc, binding site

GO Term annotation Help

Process

GO:0006801 superoxide metabolic process
GO:0055114 oxidation reduction

Function

GO:0046872 metal ion binding

InterPro annotation

Entry Details in BioMart

Abstract

Superoxide dismutases are ubiquitous metalloproteins that prevent damage by oxygen-mediated free radicals by catalysing the dismutation of superoxide into molecular oxygen and hydrogen peroxide [1]. Superoxide is a normal by-product of aerobic respiration and is produced by a number of reactions, including oxidative phosphorylation and photosynthesis. The dismutase enzymes have a very high catalytic efficiency due to the attraction of superoxide to the ions bound at the active site [2, 3].

There are three forms of superoxide dismutase, depending on the metal cofactor: Cu/Zn (which binds both copper and zinc), Fe and Mn types. The Fe and Mn forms are similar in their primary, secondary and tertiary structures, but are distinct from the Cu/Zn form [4]. Prokaryotes and protists contain Mn, Fe or both types, while most eukaryotic organisms utilise the Cu/Zn type.

Structural links Help

PDB - click here

SCOP: b.1.8.1

CATH: 2.60.40.200

Database links Help

PDBe-motif: PS00087 , PS00332

Enzyme: EC:1.15.1.1

PROSITE doc: PDOC00082

PANDIT: PF00080

Blocks: IPB001424

COMe: PRX000481

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001424

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O09164 Extracellular superoxide dismutase [Cu-Zn]

O14618 Copper chaperone for superoxide dismutase

P00445 Superoxide dismutase [Cu-Zn]

P34461 Extracellular superoxide dismutase [Cu-Zn]

P61851 Superoxide dismutase [Cu-Zn]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006121	Heavy metal transport/detoxification protein
IPR018152	Superoxide dismutase, copper/zinc, binding site
IPR001424	Superoxide dismutase, copper/zinc binding
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Schinina ME, Barra D, Bossa F, Calabrese L, Montesano L, Carri MT, Mariottini P, Amaldi F, Rotilio G. Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis. Arch. Biochem. Biophys. 272 507-15 1989 [PubMed: 2751312] http://dx.doi.org/10.1016/0003-9861(89)90246-4
2.	Parge HE, Hallewell RA, Tainer JA. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 89 6109-13 1992 [PubMed: 1463506] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1463506&action=stream&blobtype=pdf
3.	Schinina ME, Barra D, Simmaco M, Bossa F, Rotilio G. Primary structure of porcine Cu,Zn superoxide dismutase. FEBS Lett. 186 267-70 1985 [PubMed: 3891411] http://dx.doi.org/10.1016/0014-5793(85)80722-5
4.	Van Camp W, Bowler C, Villarroel R, Tsang EW, Van Montagu M, Inze D. Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 87 9903-7 1990 [PubMed: 2263641] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2263641&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ. Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. J. Biol. Chem. 283 2008 16169-77 [PubMed: 18378676] http://dx.doi.org/10.1074/jbc.M801522200
	Roberts BR, Tainer JA, Getzoff ED, Malencik DA, Anderson SR, Bomben VC, Meyers KR, Karplus PA, Beckman JS. Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS. J. Mol. Biol. 373 2007 877-90 [PubMed: 17888947] http://dx.doi.org/10.1016/j.jmb.2007.07.043
	Yogavel M, Gill J, Mishra PC, Sharma A. SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution. Acta Crystallogr. D Biol. Crystallogr. 63 2007 931-4 [PubMed: 17642520] http://dx.doi.org/10.1107/S0907444907029174
	Hornberg A, Logan DT, Marklund SL, Oliveberg M. The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. J. Mol. Biol. 365 2007 333-42 [PubMed: 17070542] http://dx.doi.org/10.1016/j.jmb.2006.09.048
	Wang J, Caruano-Yzermans A, Rodriguez A, Scheurmann JP, Slunt HH, Cao X, Gitlin J, Hart PJ, Borchelt DR. Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability. J. Biol. Chem. 282 2007 345-52 [PubMed: 17092942] http://dx.doi.org/10.1074/jbc.M604503200

InterPro 23.1