Annotations: 1A7U

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1a7ua_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Haloperoxidase	Chloroperoxidase T	(Kitasatospora aureofaciens ) [TaxId: 1894 ],	SCOPe (2.08)
B	d1a7ub_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Haloperoxidase	Chloroperoxidase T	(Kitasatospora aureofaciens ) [TaxId: 1894 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8032544	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032544	3000102	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	Hydrolase_4_1	e1a7uA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)
B	Hydrolase_4_1	e1a7uB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00561	alpha/beta hydrolase fold (Abhydrolase_1)	alpha/beta hydrolase fold	This catalytic domain is found in a very wide range of enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	CHLOROPEROXIDASE T	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 chloride peroxidase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000639	Epoxide hydrolase-like	Family
A, B	IPR000073	Alpha/beta hydrolase fold-1	Domain
A, B	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	chloride peroxidase (cofactor free) M-CSA #248	Chloroperoxidase is a member of the non-haem type haloperoxidases. Haloperoxidases catalyse the halogenation of organic compounds in the presence of halide ions and peroxides such as hydrogen peroxide. They are named after the most electronegative halide they are able to oxidise. The enzyme also oxidises bromide and iodide. This entry represents the so-called cofactor free haloperoxidases that possess a Ser-His-Asp catalytic triad and require a short aliphatic acid (e.g. ethanoic acid) for activity. They belong to the alpha/beta hydrolase superfamily.	Defined by 5 residues: PHE:A-32SER:A-98MET:A-99ASP:A-228HIS:A-257 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.11.1.10 (PDB Primary Data) Search M-CSA Motif + EC 1.11.1.10

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.