1ISC

STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1isca1	All alpha proteins	Long alpha-hairpin	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe superoxide dismutase (FeSOD)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1isca2	Alpha and beta proteins (a+b)	Fe,Mn superoxide dismutase (SOD), C-terminal domain	Fe,Mn superoxide dismutase (SOD), C-terminal domain	Fe,Mn superoxide dismutase (SOD), C-terminal domain	Fe superoxide dismutase (FeSOD)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1iscb1	All alpha proteins	Long alpha-hairpin	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe superoxide dismutase (FeSOD)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1iscb2	Alpha and beta proteins (a+b)	Fe,Mn superoxide dismutase (SOD), C-terminal domain	Fe,Mn superoxide dismutase (SOD), C-terminal domain	Fe,Mn superoxide dismutase (SOD), C-terminal domain	Fe superoxide dismutase (FeSOD)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Fe, Mn superoxide dismutase (SOD), C-terminal domain	8022681	4001146	SCOP2 (2022-06-29)
A	SCOP2 Family	Fe, Mn superoxide dismutase (SOD), N-terminal domain	8023952	4000630	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Fe, Mn superoxide dismutase (SOD), C-terminal domain	8035061	3000916	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Fe, Mn superoxide dismutase (SOD), N-terminal domain	8036331	3000794	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Fe, Mn superoxide dismutase (SOD), N-terminal domain	8036331	3000794	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Fe, Mn superoxide dismutase (SOD), C-terminal domain	8035061	3000916	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Sod_Fe_N	e1iscA1	A: alpha bundles	X: Long alpha-hairpin	H: Fe,Mn superoxide dismutase (SOD), N-terminal domain (From Topology)	T: Fe,Mn superoxide dismutase (SOD), N-terminal domain	F: Sod_Fe_N	ECOD (1.6)
A	Sod_Fe_C	e1iscA2	A: a+b three layers	X: Fe,Mn superoxide dismutase (SOD)-C (From Topology)	H: Fe,Mn superoxide dismutase (SOD)-C (From Topology)	T: Fe,Mn superoxide dismutase (SOD)-C	F: Sod_Fe_C	ECOD (1.6)
B	Sod_Fe_N	e1iscB1	A: alpha bundles	X: Long alpha-hairpin	H: Fe,Mn superoxide dismutase (SOD), N-terminal domain (From Topology)	T: Fe,Mn superoxide dismutase (SOD), N-terminal domain	F: Sod_Fe_N	ECOD (1.6)
B	Sod_Fe_C	e1iscB2	A: a+b three layers	X: Fe,Mn superoxide dismutase (SOD)-C (From Topology)	H: Fe,Mn superoxide dismutase (SOD)-C (From Topology)	T: Fe,Mn superoxide dismutase (SOD)-C	F: Sod_Fe_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00081	Iron/manganese superoxide dismutases, alpha-hairpin domain (Sod_Fe_N)	Iron/manganese superoxide dismutases, alpha-hairpin domain	superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytopla ...	superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error?	Domain
A, B	PF02777	Iron/manganese superoxide dismutases, C-terminal domain (Sod_Fe_C)	Iron/manganese superoxide dismutases, C-terminal domain	superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplas ...	superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. C-terminal domain is a mixed alpha/beta fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	IRON(III) SUPEROXIDE DISMUTASE	oxidoreductase activity catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding superoxide dismutase activity oxidoreductase activity, acting on superoxide radicals as acceptor antioxidant activity	cellular response to stimulus response to stimulus cellular response to oxidative stress detoxification reactive oxygen species metabolic process cellular response to chemical stress response to superoxide cellular oxidant detoxification cellular response to oxygen radical cellular response to reactive oxygen species cellular response to stress response to stress cellular detoxification response to oxygen-containing compound cellular response to stimulus response to stimulus cellular response to oxidative stress detoxification reactive oxygen species metabolic process cellular response to chemical stress response to superoxide cellular oxidant detoxification cellular response to oxygen radical cellular response to reactive oxygen species cellular response to stress response to stress cellular detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to reactive oxygen species response to toxic substance removal of superoxide radicals superoxide metabolic process response to oxidative stress cellular response to chemical stimulus response to chemical cellular response to superoxide metabolic process cellular process cellular response to toxic substance response to oxygen radical	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036324	Manganese/iron superoxide dismutase, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR001189	Manganese/iron superoxide dismutase	Family
A, B	IPR019833	Manganese/iron superoxide dismutase, binding site	Binding Site
A, B	IPR019832	Manganese/iron superoxide dismutase, C-terminal	Domain
A, B	IPR019831	Manganese/iron superoxide dismutase, N-terminal	Domain
A, B	IPR036314	Manganese/iron superoxide dismutase, C-terminal domain superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.