5AA6

Homohexameric Structure of the second Vanadate-Dependent Bromoperoxidase (AnII) from Ascophyllum nodosum

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d5aa6a_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	automated matches	automated matches	(Ascophyllum nodosum ) [TaxId: 52969 ],	SCOPe (2.08)
B	d5aa6b_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	automated matches	automated matches	(Ascophyllum nodosum ) [TaxId: 52969 ],	SCOPe (2.08)
C	d5aa6c_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	automated matches	automated matches	(Ascophyllum nodosum ) [TaxId: 52969 ],	SCOPe (2.08)
D	d5aa6d_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	automated matches	automated matches	(Ascophyllum nodosum ) [TaxId: 52969 ],	SCOPe (2.08)
E	d5aa6e_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	automated matches	automated matches	(Ascophyllum nodosum ) [TaxId: 52969 ],	SCOPe (2.08)
F	d5aa6f_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	automated matches	automated matches	(Ascophyllum nodosum ) [TaxId: 52969 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Haloperoxidase (bromoperoxidase)	8083419	4001228	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8083420	3001110	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8083420	3001110	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8083420	3001110	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8083420	3001110	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8083420	3001110	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8083420	3001110	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	F_UNCLASSIFIED	e5aa6A1	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e5aa6B1	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e5aa6C1	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: F_UNCLASSIFIED	ECOD (1.6)
D	F_UNCLASSIFIED	e5aa6D1	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: F_UNCLASSIFIED	ECOD (1.6)
E	F_UNCLASSIFIED	e5aa6E1	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: F_UNCLASSIFIED	ECOD (1.6)
F	F_UNCLASSIFIED	e5aa6F1	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)
B	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)
C	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)
D	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)
E	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)
F	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	VANADIUM-DEPENDENT BROMOPEROXIDASE 2	peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR036938	Phosphatidic acid phosphatase type 2/haloperoxidase superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR016119	Bromoperoxidase/chloroperoxidase C-terminal	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.