Annotations: 5J9B

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d5j9bb1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Aspergillus fumigatus Af293 ) [TaxId: 330879 ],	SCOPe (2.08)
B	d5j9bb2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Aspergillus fumigatus Af293 ) [TaxId: 330879 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF08534	e5j9bA1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF08534	ECOD (1.6)
B	PF08534	e5j9bB1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF08534	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF08534	Redoxin (Redoxin)	Redoxin	This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	peroxiredoxin Asp f3	peroxidase activity oxidoreductase activity thioredoxin-dependent peroxiredoxin activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor thioredoxin peroxidase activity catalytic activity peroxiredoxin activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity IgE binding peroxidase activity oxidoreductase activity thioredoxin-dependent peroxiredoxin activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor thioredoxin peroxidase activity catalytic activity peroxiredoxin activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity IgE binding protein-containing complex binding immunoglobulin binding	cellular catabolic process catabolic process cellular metabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process cell redox homeostasis cellular homeostasis homeostatic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus cellular catabolic process catabolic process cellular metabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process cell redox homeostasis cellular homeostasis homeostatic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus response to stimulus cellular response to stress response to stress response to chemical cellular response to oxidative stress cellular response to chemical stress	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle peroxisome microbody

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013766	Thioredoxin domain	Domain
A, B	IPR037944	Peroxiredoxin-5-like	Family
A, B	IPR013740	Redoxin	Domain
A, B	IPR036249	Thioredoxin-like 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 R01GM133198.