Annotations: 1KKC

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1kkca1	All alpha proteins	Long alpha-hairpin	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
A	d1kkca2	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	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
B	d1kkcb1	All alpha proteins	Long alpha-hairpin	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
B	d1kkcb2	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	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
C [auth X]	d1kkcx1	All alpha proteins	Long alpha-hairpin	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
C [auth X]	d1kkcx2	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	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
D [auth Y]	d1kkcy1	All alpha proteins	Long alpha-hairpin	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Fe,Mn superoxide dismutase (SOD), N-terminal domain	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)
D [auth Y]	d1kkcy2	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	Mn superoxide dismutase (MnSOD)	(Aspergillus fumigatus ) [TaxId: 746128 ],	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) N-terminal domain	8025909	4000630	SCOP2 (2022-06-29)
A	SCOP2 Family	Fe Mn superoxide dismutase (SOD) C-terminal domain	8025911	4001146	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Fe Mn superoxide dismutase (SOD) N-terminal domain	8038288	3000794	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Fe Mn superoxide dismutase (SOD) C-terminal domain	8038290	3000916	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Fe Mn superoxide dismutase (SOD) N-terminal domain	8038288	3000794	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Fe Mn superoxide dismutase (SOD) C-terminal domain	8038290	3000916	SCOP2B (2022-06-29)
C [auth X]	SCOP2B Superfamily	Fe Mn superoxide dismutase (SOD) N-terminal domain	8038288	3000794	SCOP2B (2022-06-29)
C [auth X]	SCOP2B Superfamily	Fe Mn superoxide dismutase (SOD) C-terminal domain	8038290	3000916	SCOP2B (2022-06-29)
D [auth Y]	SCOP2B Superfamily	Fe Mn superoxide dismutase (SOD) N-terminal domain	8038288	3000794	SCOP2B (2022-06-29)
D [auth Y]	SCOP2B Superfamily	Fe Mn superoxide dismutase (SOD) C-terminal domain	8038290	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	e1kkcA1	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	e1kkcA2	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	e1kkcB1	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	e1kkcB2	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)
C [auth X]	Sod_Fe_N	e1kkcX1	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)
C [auth X]	Sod_Fe_C	e1kkcX2	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)
D [auth Y]	Sod_Fe_N	e1kkcY1	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)
D [auth Y]	Sod_Fe_C	e1kkcY2	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.287.990	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Fe,Mn superoxide dismutase (SOD) domain	CATH (4.3.0)
A	3.55.40.20	Alpha Beta	3-Layer(bab) Sandwich	minor pseudopilin epsh fold	Iron/manganese superoxide dismutase, C-terminal domain	CATH (4.3.0)
B	1.10.287.990	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Fe,Mn superoxide dismutase (SOD) domain	CATH (4.3.0)
B	3.55.40.20	Alpha Beta	3-Layer(bab) Sandwich	minor pseudopilin epsh fold	Iron/manganese superoxide dismutase, C-terminal domain	CATH (4.3.0)
C [auth X]	1.10.287.990	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Fe,Mn superoxide dismutase (SOD) domain	CATH (4.3.0)
C [auth X]	3.55.40.20	Alpha Beta	3-Layer(bab) Sandwich	minor pseudopilin epsh fold	Iron/manganese superoxide dismutase, C-terminal domain	CATH (4.3.0)
D [auth Y]	1.10.287.990	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Fe,Mn superoxide dismutase (SOD) domain	CATH (4.3.0)
D [auth Y]	3.55.40.20	Alpha Beta	3-Layer(bab) Sandwich	minor pseudopilin epsh fold	Iron/manganese superoxide dismutase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C [auth X], D [auth Y]	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, C [auth X], D [auth Y]	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, C [auth X], D [auth Y]	Manganese Superoxide Dismutase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding IgE binding protein-containing complex binding immunoglobulin binding superoxide dismutase activity oxidoreductase activity, acting on superoxide radicals as acceptor oxidoreductase activity antioxidant activity cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding IgE binding protein-containing complex binding immunoglobulin binding superoxide dismutase activity oxidoreductase activity, acting on superoxide radicals as acceptor oxidoreductase activity antioxidant activity catalytic activity	-	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

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

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.