Annotations: 3E6R

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3e6ra_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Non-hem ferritin	(Pseudo-nitzschia multiseries ) [TaxId: 37319 ],	SCOPe (2.08)
B	d3e6rb_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Non-hem ferritin	(Pseudo-nitzschia multiseries ) [TaxId: 37319 ],	SCOPe (2.08)
C	d3e6rc_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Non-hem ferritin	(Pseudo-nitzschia multiseries ) [TaxId: 37319 ],	SCOPe (2.08)
D	d3e6rd_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Non-hem ferritin	(Pseudo-nitzschia multiseries ) [TaxId: 37319 ],	SCOPe (2.08)
E	d3e6re_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Non-hem ferritin	(Pseudo-nitzschia multiseries ) [TaxId: 37319 ],	SCOPe (2.08)
F	d3e6rf_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Non-hem ferritin	(Pseudo-nitzschia multiseries ) [TaxId: 37319 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ferritin-like	8063912	3001658	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ferritin-like	8063912	3001658	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ferritin-like	8063912	3001658	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Ferritin-like	8063912	3001658	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Ferritin-like	8063912	3001658	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Ferritin-like	8063912	3001658	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	PF00210	e3e6rA1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: PF00210	ECOD (1.6)
B	PF00210	e3e6rB1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: PF00210	ECOD (1.6)
C	PF00210	e3e6rC1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: PF00210	ECOD (1.6)
D	PF00210	e3e6rD1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: PF00210	ECOD (1.6)
E	PF00210	e3e6rE1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: PF00210	ECOD (1.6)
F	PF00210	e3e6rF1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: PF00210	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
B	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
C	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
D	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
E	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
F	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00210	Ferritin-like domain (Ferritin)	Ferritin-like domain	This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Ferritin	cation binding ferric iron binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity, acting on metal ions oxidoreductase activity ferroxidase activity oxidoreductase activity, acting on metal ions, oxygen as acceptor catalytic activity identical protein binding cation binding ferric iron binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity, acting on metal ions oxidoreductase activity ferroxidase activity oxidoreductase activity, acting on metal ions, oxygen as acceptor catalytic activity identical protein binding protein binding	intracellular iron ion homeostasis inorganic ion homeostasis cellular homeostasis chemical homeostasis homeostatic process intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis localization transport iron ion transport transition metal ion transport intracellular iron ion homeostasis inorganic ion homeostasis cellular homeostasis chemical homeostasis homeostatic process intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis localization transport iron ion transport transition metal ion transport monoatomic ion transport monoatomic cation transport establishment of localization metal ion transport	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR009040	Ferritin-like diiron domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR041719	Ferritin, prokaryotic-type	Family
A, B, C, D, E A, B, C, D, E, F	IPR012347	Ferritin-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR009078	Ferritin-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR001519	Ferritin	Family
A, B, C, D, E A, B, C, D, E, F	IPR008331	Ferritin/DPS protein domain	Domain

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.