Annotations: 4Q5F

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4q5fa2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Pig roundworm (Ascaris suum ) [TaxId: 6253 ],	SCOPe (2.08)
A	d4q5fa1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Pig roundworm (Ascaris suum ) [TaxId: 6253 ],	SCOPe (2.08)
B [auth D]	d4q5fd2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Pig roundworm (Ascaris suum ) [TaxId: 6253 ],	SCOPe (2.08)
B [auth D]	d4q5fd1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Pig roundworm (Ascaris suum ) [TaxId: 6253 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF14497	e4q5fA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF14497	ECOD (1.6)
A	PF02798	e4q5fA1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF02798	ECOD (1.6)
B [auth D]	PF14497	e4q5fD1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF14497	ECOD (1.6)
B [auth D]	PF02798	e4q5fD2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF02798	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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)
B [auth D]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B [auth D]	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 [auth D]	PF14497	Glutathione S-transferase, C-terminal domain (GST_C_3)	Glutathione S-transferase, C-terminal domain	This domain is closely related to Pfam:PF00043.	Domain
A, B [auth D]	PF02798	Glutathione S-transferase, N-terminal domain (GST_N)	Glutathione S-transferase, N-terminal domain	Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity a ...	Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognised); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognised). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth D]	Glutathione S-transferase 1	glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor glutathione peroxidase activity	cellular response to stimulus cellular detoxification cellular response to chemical stimulus response to stimulus response to chemical detoxification cellular process cellular oxidant detoxification cellular response to toxic substance response to toxic substance	cellular anatomical entity cluster of actin-based cell projections brush border intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth D]	IPR004046	Glutathione S-transferase, C-terminal	Domain
A, B [auth D]	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B [auth D]	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A, B [auth D]	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B [auth D]	IPR036249	Thioredoxin-like superfamily	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.