Annotations: 1QHB

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qhba_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Haloperoxidase (bromoperoxidase)	Haloperoxidase (bromoperoxidase)	(Corallina officinalis ) [TaxId: 35170 ],	SCOPe (2.08)
B	d1qhbb_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Haloperoxidase (bromoperoxidase)	Haloperoxidase (bromoperoxidase)	(Corallina officinalis ) [TaxId: 35170 ],	SCOPe (2.08)
D	d1qhbd_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Haloperoxidase (bromoperoxidase)	Haloperoxidase (bromoperoxidase)	(Corallina officinalis ) [TaxId: 35170 ],	SCOPe (2.08)
C	d1qhbc_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Haloperoxidase (bromoperoxidase)	Haloperoxidase (bromoperoxidase)	(Corallina officinalis ) [TaxId: 35170 ],	SCOPe (2.08)
E	d1qhbe_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Haloperoxidase (bromoperoxidase)	Haloperoxidase (bromoperoxidase)	(Corallina officinalis ) [TaxId: 35170 ],	SCOPe (2.08)
F	d1qhbf_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Haloperoxidase (bromoperoxidase)	Haloperoxidase (bromoperoxidase)	(Corallina officinalis ) [TaxId: 35170 ],	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)	8026117	4001228	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038496	3001110	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038496	3001110	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038496	3001110	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038496	3001110	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038496	3001110	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038496	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	PAP2	e1qhbA1	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: PAP2	ECOD (1.6)
B	PAP2	e1qhbB1	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: PAP2	ECOD (1.6)
D	PAP2	e1qhbD1	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: PAP2	ECOD (1.6)
C	PAP2	e1qhbC1	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: PAP2	ECOD (1.6)
E	PAP2	e1qhbE1	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: PAP2	ECOD (1.6)
F	PAP2	e1qhbF1	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: PAP2	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)
D	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)
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	HALOPEROXIDASE	peroxidase activity haloperoxidase activity oxidoreductase activity halogenase activity antioxidant activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on peroxide as acceptor catalytic activity bromide peroxidase activity cation binding ion binding binding metal ion binding small molecule binding	-	-

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
A, B, C, D, E A, B, C, D, E, F	IPR052559	Vanadium-dependent haloperoxidase	Family

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.