5A4W

AtGSTF2 from Arabidopsis thaliana in complex with quercetrin

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d5a4wa2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
A	d5a4wa1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d5a4wb2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d5a4wb1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
D	d5a4wd2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
D	d5a4wd1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
E	d5a4we2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
E	d5a4we1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
C	d5a4wc2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
C	d5a4wc1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
F	d5a4wf2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
F	d5a4wf1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	automated matches	THALE CRESS (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GST C-terminal domain-like	8037556	3000305	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thioredoxin-like	8044380	3000031	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GST C-terminal domain-like	8037556	3000305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8044380	3000031	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	GST C-terminal domain-like	8037556	3000305	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin-like	8044380	3000031	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioredoxin-like	8044380	3000031	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	GST C-terminal domain-like	8037556	3000305	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin-like	8044380	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GST C-terminal domain-like	8037556	3000305	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	GST C-terminal domain-like	8037556	3000305	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioredoxin-like	8044380	3000031	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	GST_C_3	e5a4wA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
A	GST_N	e5a4wA1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
B	GST_C_3	e5a4wB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
B	GST_N	e5a4wB2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
D	GST_C_3	e5a4wD2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
D	GST_N	e5a4wD1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
E	GST_C_3	e5a4wE2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
E	GST_N	e5a4wE1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
C	GST_C_3	e5a4wC1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
C	GST_N	e5a4wC2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
F	GST_C_3	e5a4wF2	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
F	GST_N	e5a4wF1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	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)
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)
E	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
E	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)
F	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
F	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, E A, B, C, D, E, F	PF00043	Glutathione S-transferase, C-terminal domain (GST_C)	Glutathione S-transferase, C-terminal domain	GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins ...	GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain [1]. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes [2].	Domain
A, B, C, D, E A, B, C, D, E, F	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, E A, B, C, D, E, F	GLUTATHIONE S-TRANSFERASE F2	protein binding binding protein domain specific binding peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity organic cyclic compound binding camalexin binding sulfur compound binding amide binding modified amino acid binding ion binding protein binding binding protein domain specific binding peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity organic cyclic compound binding camalexin binding sulfur compound binding amide binding modified amino acid binding ion binding oligopeptide binding anion binding glutathione binding small molecule binding salicylic acid binding organic acid binding carboxylic acid binding monocarboxylic acid binding glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups quercitrin binding flavonoid binding carbohydrate derivative binding	response to stimulus response to stress response to abiotic stimulus response to cold response to temperature stimulus defense response response to metal ion response to chemical response to zinc ion catabolic process detoxification response to toxic substance secondary metabolic process cellular catabolic process response to stimulus response to stress response to abiotic stimulus response to cold response to temperature stimulus defense response response to metal ion response to chemical response to zinc ion catabolic process detoxification response to toxic substance secondary metabolic process cellular catabolic process toxin catabolic process metabolic process cellular process toxin metabolic process response to cadmium ion biological process involved in interspecies interaction between organisms response to oomycetes response to other organism response to external stimulus response to external biotic stimulus response to biotic stimulus auxin-activated signaling pathway cellular response to stimulus regulation of biological process regulation of cellular process signaling response to endogenous stimulus biological regulation hormone-mediated signaling pathway cellular response to auxin stimulus cell communication response to auxin cellular response to endogenous stimulus cellular response to chemical stimulus response to hormone signal transduction cellular response to hormone stimulus	membrane-bounded organelle intracellular anatomical structure plastid intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure plastid stroma organelle chloroplast stroma cytoplasm chloroplast cytosol cell periphery plasma membrane membrane-bounded organelle intracellular anatomical structure plastid intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure plastid stroma organelle chloroplast stroma cytoplasm chloroplast cytosol cell periphery plasma membrane membrane extracellular region apoplast plant-type vacuole vacuole cell-cell junction symplast anchoring junction cell junction plasmodesma endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR004046	Glutathione S-transferase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B, C, D, E A, B, C, D, E, F	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR034347	Glutathione S-transferases Phi, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	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 R01GM157729.