Annotations: 3VXI

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3vxia_	Alpha and beta proteins (a+b)	Ferredoxin-like	Dimeric alpha+beta barrel	Dyp-type peroxidase-like	Decolorizing peroxidase DyP	(Bjerkandera adusta ) [TaxId: 5331 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dimeric alpha+beta barrel	8039544	3000089	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Dimeric alpha+beta barrel	8090936	3000089	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	Dyp_perox_N	e3vxiA2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N	ECOD (1.6)
A	Dyp_perox_C	e3vxiA3	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF20628	Dyp-type peroxidase, C-terminal (Dyp_perox_C)	Dyp-type peroxidase, C-terminal	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much ...	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much lower pH conditions compared with the other plant peroxidases [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the C-terminal domain, which possess a large hydrophobic cavity for heme binding [2,3,4].	Domain
A	PF21105	DyP dimeric alpha+beta barrel domain (DyP_N)	DyP dimeric alpha+beta barrel domain	This entry represents the N-terminal dimeric alpha beta barrel domain from the dye-decolorizing peroxidase (DyP)-type peroxidase family. This is one of the six families of peroxidases [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DyP	peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	-	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR049509	DyP dimeric alpha+beta barrel domain	Domain
A	IPR006314	Dyp-type peroxidase	Family
A	IPR048328	Dyp-type peroxidase, C-terminal domain	Domain
A	IPR011008	Dimeric alpha-beta barrel	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 R01GM157729.