5G5A

Glutathione transferase U25 from Arabidopsis thaliana in complex with glutathione disulfide

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
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	d5g5aa2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
A	d5g5aa1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d5g5ab2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d5g5ab1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
C	d5g5ac2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
C	d5g5ac1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
D	d5g5ad2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
D	d5g5ad1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	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	PF13410	e5g5aA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF13410	ECOD (1.6)
A	PF02798	e5g5aA2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF02798	ECOD (1.6)
B	PF13410	e5g5aB2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF13410	ECOD (1.6)
B	PF02798	e5g5aB1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF02798	ECOD (1.6)
C	PF13410	e5g5aC2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF13410	ECOD (1.6)
C	PF02798	e5g5aC1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF02798	ECOD (1.6)
D	PF13410	e5g5aD2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF13410	ECOD (1.6)
D	PF02798	e5g5aD1	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	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)
C	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
C	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)
D	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
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, C, D	PF13410	Glutathione S-transferase, C-terminal domain (GST_C_2)	Glutathione S-transferase, C-terminal domain	This domain is closely related to Pfam:PF00043.	Domain
A, B, C, 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, C, D	GLUTATHIONE S-TRANSFERASE U25	glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	2,4,6-trinitrotoluene catabolic process catabolic process benzene-containing compound metabolic process trinitrotoluene metabolic process nitrotoluene catabolic process trinitrotoluene catabolic process toluene-containing compound metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process 2,4,6-trinitrotoluene metabolic process metabolic process nitrotoluene metabolic process toluene-containing compound catabolic process 2,4,6-trinitrotoluene catabolic process catabolic process benzene-containing compound metabolic process trinitrotoluene metabolic process nitrotoluene catabolic process trinitrotoluene catabolic process toluene-containing compound metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process 2,4,6-trinitrotoluene metabolic process metabolic process nitrotoluene metabolic process toluene-containing compound catabolic process organic substance catabolic process response to stimulus detoxification cellular metabolic process response to toxic substance secondary metabolic process cellular catabolic process toxin catabolic process response to chemical cellular process toxin metabolic process glutathione metabolic process organonitrogen compound metabolic process sulfur compound metabolic process amide metabolic process cellular modified amino acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B, C, D	IPR045073	Glutathione S-transferase Omega/Tau-like	Family
A, B, C, D	IPR045074	Glutathione S-transferases Tau, C-terminal alpha helical domain, plant	Domain
A, B, C, D	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B, C, 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.