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InterPro: IPR018152 Superoxide dismutase, copper/zinc, binding site

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1327 proteins

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Accession

IPR018152 SOD_Cu/Zn_BS

Type

Binding_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00087	SOD_CU_ZN_1	961
PROSITE pattern	PS00332	SOD_CU_ZN_2	1159
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001424 Superoxide dismutase, copper/zinc binding

InterPro annotation

Entry Details in BioMart

Abstract

Copper/Zinc superoxide dismutase (SODC) [1] is one of the three forms of an enzyme that catalyzes the dismutation of superoxide radicals. SODC binds one atom each of zinc and copper. Various forms of SODC are known: a cytoplasmic form in eukaryotes, an additional chloroplast form in plants, an extracellular form in some eukaryotes, and a periplasmic form in prokaryotes. The metal binding sites are conserved in all the known SODC sequences [2].

This entry contains 2 patterns, the first contains the two histidine residues that bind the copper atom; the second one is located in the C-terminal section of SODC and contains a cysteine which is involved in a disulphide bond. These patterns will not detect proteins related to SODC, but which have lost their catalytic activity, such as Vaccinia virus protein A45.

Structural links Help

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SCOP: b.1.8.1

CATH: 2.60.40.200

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Enzyme: EC:1.15.1.1

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Overlapping InterPro entries Help

IPR018152

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.	Bannister JV, Bannister WH, Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit. Rev. Biochem. 22 111-80 1987 [PubMed: 3315461]
2.	Beresky MA, Hall DW. The influence of phenylthiourea on encapsulation, melanization, and survival in larvae of the mosquito Aedes aegypti parasitized by the nematode Neoaplectana carpocapsae. J. Invertebr. Pathol. 29 74-80 1977 [PubMed: 556751] http://dx.doi.org/10.1016/0022-2011(77)90175-6

Additional Reading Open in usermanual
	Strange RW, Yong CW, Smith W, Hasnain SS. Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 104 2007 10040-4 [PubMed: 17548825] http://dx.doi.org/10.1073/pnas.0703857104
	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
	Smith MW, Doolittle RF. A comparison of evolutionary rates of the two major kinds of superoxide dismutase. J. Mol. Evol. 34 1992 175-84 [PubMed: 1556751]

InterPro 23.1