2YW6

Structural studies of N terminal deletion mutant of Dps from Mycobacterium smegmatis

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	d2yw6a_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Dodecameric ferritin homolog	(Mycolicibacterium smegmatis ) [TaxId: 1772 ],	SCOPe (2.08)
B	d2yw6b_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Dodecameric ferritin homolog	(Mycolicibacterium smegmatis ) [TaxId: 1772 ],	SCOPe (2.08)
C	d2yw6c_	All alpha proteins	Ferritin-like	Ferritin-like	Ferritin	Dodecameric ferritin homolog	(Mycolicibacterium smegmatis ) [TaxId: 1772 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Ferritin	8025537	4000839	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Ferritin-like	8037916	3001658	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Ferritin-like	8037916	3001658	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ferritin-like	8037916	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	e2yw6A1	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	e2yw6B1	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	e2yw6C1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	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	DNA protection during starvation protein	DNA binding binding organic cyclic compound binding nucleic acid binding oxidoreductase activity, acting on metal ions oxidoreductase activity catalytic activity cation binding ferric iron binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule 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	nucleoid cellular anatomical entity intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR012347	Ferritin-like	Homologous Superfamily
A, B, C	IPR009078	Ferritin-like superfamily	Homologous Superfamily
A, B, C	IPR002177	DNA-binding protein Dps	Family
A, B, C	IPR023188	DNA-binding protein Dps, conserved site	Conserved Site
A, B, C	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.