Annotations: 5Y7I

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d5y7ib2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	(Oreochromis mossambicus ) [TaxId: 8127 ],	SCOPe (2.08)
B	d5y7ib1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Oreochromis mossambicus ) [TaxId: 8127 ],	SCOPe (2.08)
A	d5y7ia2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	(Oreochromis mossambicus ) [TaxId: 8127 ],	SCOPe (2.08)
A	d5y7ia1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Oreochromis mossambicus ) [TaxId: 8127 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	F_UNCLASSIFIED	e5y7iB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF22441	e5y7iB2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF22441	ECOD (1.6)
A	F_UNCLASSIFIED	e5y7iA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF22441	e5y7iA1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF22441	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
A	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13409	Glutathione S-transferase, N-terminal domain (GST_N_2)	Glutathione S-transferase, N-terminal domain	This family is closely related to Pfam:PF02798.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	chloride intracellular channel protein 2	monoatomic anion transmembrane transporter activity chloride transmembrane transporter activity monoatomic ion channel activity passive transmembrane transporter activity inorganic molecular entity transmembrane transporter activity channel activity monoatomic anion channel activity monoatomic ion transmembrane transporter activity transporter activity transmembrane transporter activity inorganic anion transmembrane transporter activity chloride channel activity	-	protein-containing complex transmembrane transporter complex membrane chloride channel complex membrane protein complex cellular anatomical entity transporter complex monoatomic ion channel complex intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B	IPR030253	Chloride intracellular channel protein 2, C-terminal domain	Domain
A, B	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A, B	IPR002946	Intracellular chloride channel	Family
A, B	IPR040079	Glutathione transferase family	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 R01GM133198.