5XGO

The Ferritin E-Domain: Toward Understanding Its Role in Protein Cage Assembly Through the Crystal Structure of a Maxi-/Mini-Ferritin Chimera

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d5xgoa_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d5xgob_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d5xgoc_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
D	d5xgod_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
E	d5xgoe_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
F	d5xgof_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
G	d5xgog_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
H	d5xgoh_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
I	d5xgoi_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
J	d5xgoj_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
K	d5xgok_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
L	d5xgol_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Bacterioferritin (cytochrome b1)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	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	8036995	3001658	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Ferritin-like	8036995	3001658	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Ferritin-like	8036995	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	Ferritin_1	e5xgoA1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
B	Ferritin_1	e5xgoB1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
C	Ferritin_1	e5xgoC1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
D	Ferritin_1	e5xgoD1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
E	Ferritin_1	e5xgoE1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
F	Ferritin_1	e5xgoF1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
G	Ferritin_1	e5xgoG1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
H	Ferritin_1	e5xgoH1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
I	Ferritin_1	e5xgoI1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
J	Ferritin_1	e5xgoJ1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
K	Ferritin_1	e5xgoK1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	ECOD (1.6)
L	Ferritin_1	e5xgoL1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Ferritin	F: Ferritin_1	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)
G	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
H	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
I	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
J	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
K	1.20.1260.10	Mainly Alpha	Up-down Bundle	Ferritin	Ferritin, core subunit, four-helix bundle	CATH (4.3.0)
L	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, G, H, I, J, K, L	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, G, H, I, J, K, L	DNA protection during starvation protein,Bacterioferritin	oxidoreductase activity catalytic activity molecular sequestering activity iron ion sequestering activity metal ion sequestering activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity monoatomic cation transmembrane transporter activity inorganic molecular entity transmembrane transporter activity iron ion transmembrane transporter activity inorganic cation transmembrane transporter activity oxidoreductase activity catalytic activity molecular sequestering activity iron ion sequestering activity metal ion sequestering activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity monoatomic cation transmembrane transporter activity inorganic molecular entity transmembrane transporter activity iron ion transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity ferrous iron transmembrane transporter activity transporter activity transition metal ion transmembrane transporter activity metal ion transmembrane transporter activity transmembrane transporter activity cation binding ferric iron binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding tetrapyrrole binding heme binding oxidoreductase activity, acting on metal ions ferroxidase activity oxidoreductase activity, acting on metal ions, oxygen as acceptor DNA binding nucleic acid 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 regulation of DNA-templated DNA replication initiation regulation of cellular process negative regulation of biological process negative regulation of DNA-templated DNA replication initiation 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 regulation of DNA-templated DNA replication initiation regulation of cellular process negative regulation of biological process negative regulation of DNA-templated DNA replication initiation regulation of primary metabolic process nucleobase-containing compound metabolic process negative regulation of DNA-templated DNA replication negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process negative regulation of macromolecule metabolic process DNA-templated DNA replication regulation of biological process negative regulation of DNA replication DNA replication initiation negative regulation of metabolic process biological regulation primary metabolic process DNA metabolic process regulation of macromolecule metabolic process nucleic acid metabolic process DNA replication regulation of DNA-templated DNA replication metabolic process cellular process negative regulation of DNA metabolic process macromolecule metabolic process regulation of metabolic process regulation of DNA replication regulation of DNA metabolic process cellular component organization organelle organization chromosome condensation chromosome organization cellular component organization or biogenesis response to stimulus response to stress response to nutrient levels response to starvation	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol protein-containing complex DnaA-Dps complex protein-DNA complex intracellular membraneless organelle chromosome replication inhibiting complex intracellular organelle organelle membraneless organelle cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol protein-containing complex DnaA-Dps complex protein-DNA complex intracellular membraneless organelle chromosome replication inhibiting complex intracellular organelle organelle membraneless organelle replication fork replisome nucleoid

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR009040	Ferritin-like diiron domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR002024	Bacterioferritin	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR012347	Ferritin-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR009078	Ferritin-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR008331	Ferritin/DPS domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR002177	DNA-binding protein Dps	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR012347	Ferritin-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR009078	Ferritin-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR023067	DNA protection during starvation protein, gammaproteobacteria	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR008331	Ferritin/DPS domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR023188	DNA-binding protein Dps, conserved site	Conserved Site

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.