7B74

Chimeric Streptavidin With A Dimerization Domain For Artificial Transfer Hydrogenation

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth AAA]	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	SCOP2B (2022-06-29)
C [auth CCC]	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	SCOP2B (2022-06-29)
D [auth DDD]	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	SCOP2B (2022-06-29)
B [auth BBB]	SCOP2B Superfamily	Avidin/streptavidin	8040372	3001465	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 [auth AAA]	Avidin	e7b74AAA1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: Avidin	ECOD (1.6)
C [auth CCC]	Avidin	e7b74CCC1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: Avidin	ECOD (1.6)
D [auth DDD]	Avidin	e7b74DDD1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: Avidin	ECOD (1.6)
B [auth BBB]	Avidin	e7b74BBB1	A: beta barrels	X: Lipocalins/Streptavidin	H: Avidin/Streptavidin (From Topology)	T: Avidin/Streptavidin	F: Avidin	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	PF01382	Avidin family (Avidin)	Avidin family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	Streptavidin,Superoxide dismutase [Cu-Zn],Streptavidin	biotin binding amide binding organic acid binding binding vitamin binding ion binding organic cyclic compound binding anion binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding cation binding biotin binding amide binding organic acid binding binding vitamin binding ion binding organic cyclic compound binding anion binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding cation binding transition metal ion binding copper ion binding metal ion binding superoxide dismutase activity oxidoreductase activity, acting on superoxide radicals as acceptor oxidoreductase activity antioxidant activity catalytic activity	-	cellular anatomical structure extracellular region cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR017889	Avidin-like, conserved site	Conserved Site
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR036896	Avidin-like superfamily	Homologous Superfamily
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR051764	Avidin/Streptavidin-related	Family
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR005468	Avidin/streptavidin	Family
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR005469	Avidin	Family
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR024134	Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone	Family
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR036423	Superoxide dismutase-like, copper/zinc binding domain superfamily	Homologous Superfamily
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR018152	Superoxide dismutase, copper/zinc, binding site	Binding Site
A [auth AAA], B [auth BBB], C [auth CCC], D [auth DDD]	IPR001424	Superoxide dismutase, copper/zinc binding domain	Domain

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.