Annotations: 1DO6

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1do6a_	All beta proteins	Immunoglobulin-like beta-sandwich	Superoxide reductase-like	Superoxide reductase-like	Superoxide reductase (SOR)	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
B	d1do6b_	All beta proteins	Immunoglobulin-like beta-sandwich	Superoxide reductase-like	Superoxide reductase-like	Superoxide reductase (SOR)	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Superoxide reductase-like	8055345	3002044	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Superoxide reductase-like	8055345	3002044	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	Desulfoferrodox	e1do6A1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Desulfoferrodox	ECOD (1.6)
B	Desulfoferrodox	e1do6B1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Desulfoferrodox	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.730	Mainly Beta	Sandwich	Immunoglobulin-like	SOR catalytic domain	CATH (4.3.0)
B	2.60.40.730	Mainly Beta	Sandwich	Immunoglobulin-like	SOR catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01880	Desulfoferrodoxin (Desulfoferrodox)	Desulfoferrodoxin	Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands. Due to this ...	Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands. Due to this rather unusual combination of active centres, this novel protein is named desulfoferrodoxin [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	SUPEROXIDE REDUCTASE	oxidoreductase activity, acting on superoxide radicals as acceptor oxidoreductase activity antioxidant activity superoxide reductase activity catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036073	Desulfoferrodoxin, ferrous iron-binding domain superfamily	Homologous Superfamily
A, B	IPR002742	Desulfoferrodoxin, ferrous iron-binding domain	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	superoxide reductase M-CSA #660	Neelareductase, or superoxide reductase, from the thermophilic Archaea Pyrococcus furiosus, is able to catalyse the conversion of the superoxide radical O*- into the less toxic product hydrogen peroxide. It shares this ability with a number of homologous proteins from anaerobic bacteria and archaea where the removal of the superoxide radical, a product of anaerobic respiration in these organisms, is essential for their survival. It is part of a family of mononuclear non-haem iron containing proteins, which all have the iron coordinated with a pentacoordinate 4 His Cys motif and a variable 6th ligand.	Defined by 7 residues: GLU:A-14LYS:A-15HIS:A-16HIS:A-41HIS:A-47CYS:A-111HIS:A-114 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif

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.