1V0H

ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID

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 [auth X]	d1v0hx1	All alpha proteins	Heme-dependent peroxidases	Heme-dependent peroxidases	CCP-like	Ascorbate peroxidase	SOYBEAN (Glycine max ) [TaxId: 3847 ],	SCOPe (2.08)
A [auth X]	d1v0hx2	Artifacts	Tags	Tags	Tags	N-terminal Tags	SOYBEAN (Glycine max ) [TaxId: 3847 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth X]	SCOP2B Superfamily	Heme-dependent peroxidases	8033915	3000844	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 X]	peroxidase	e1v0hX1	A: alpha complex topology	X: Heme-dependent peroxidases (From Topology)	H: Heme-dependent peroxidases (From Topology)	T: Heme-dependent peroxidases	F: peroxidase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth X]	1.10.520.10	Mainly Alpha	Orthogonal Bundle	Peroxidase	domain 1	CATH (4.3.0)
A [auth X]	1.10.420.10	Mainly Alpha	Orthogonal Bundle	Peroxidase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth X]	PF00141	Peroxidase (peroxidase)	Peroxidase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth X]	ASCORBATE PEROXIDASE	peroxidase activity oxidoreductase activity antioxidant activity L-ascorbate peroxidase 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	catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to oxidative stress response to stimulus response to stress response to chemical response to oxygen-containing compound response to reactive oxygen species cellular response to stimulus cellular response to chemical stimulus catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to oxidative stress response to stimulus response to stress response to chemical response to oxygen-containing compound response to reactive oxygen species cellular response to stimulus cellular response to chemical stimulus cellular response to stress cellular response to oxidative stress cellular response to chemical stress	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure plastid organelle cytoplasm intracellular membrane-bounded organelle chloroplast

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth X]	IPR002016	Haem peroxidase	Domain
A [auth X]	IPR019794	Peroxidase, active site	Active Site
A [auth X]	IPR010255	Haem peroxidase superfamily	Homologous Superfamily
A [auth X]	IPR002207	Class I peroxidase	Family
A [auth X]	IPR044831	Heme-binding peroxidase Ccp1-like	Family
A [auth X]	IPR019793	Peroxidases heam-ligand binding site	Binding Site

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.