5GZZ

Crystal Structure of FIN219-SjGST complex with JA

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)
B	d5gzzb2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
B	d5gzzb1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
C	d5gzzc2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
C	d5gzzc1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
D	d5gzzd2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
D	d5gzzd1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
E	d5gzze2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
E	d5gzze1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
F	d5gzzf2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
F	d5gzzf1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
G	d5gzzg2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)
G	d5gzzg1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	Blood fluke (Schistosoma japonicum ) [TaxId: 6182 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	GST C-terminal domain-like	8037552	3000305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8044378	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GST C-terminal domain-like	8037552	3000305	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin-like	8044378	3000031	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	GST C-terminal domain-like	8037552	3000305	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin-like	8044378	3000031	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioredoxin-like	8044378	3000031	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	GST C-terminal domain-like	8037552	3000305	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioredoxin-like	8044378	3000031	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	GST C-terminal domain-like	8037552	3000305	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	GST C-terminal domain-like	8037552	3000305	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Thioredoxin-like	8044378	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)
B	GST_C_3	e5gzzB2	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_5	e5gzzB1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
C	GST_C_3	e5gzzC1	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_5	e5gzzC2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
D	GST_C_3	e5gzzD2	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_5	e5gzzD1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
E	GST_C_3	e5gzzE1	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_5	e5gzzE2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
F	GST_C_3	e5gzzF2	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_5	e5gzzF1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
G	GST_C_3	e5gzzG2	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)
G	GST_N_5	e5gzzG1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
A	GH3_2nd	e5gzzA1	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: GH3_2nd	ECOD (1.6)
A	GH3_3rd	e5gzzA3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: GH3_3rd	ECOD (1.6)
A	GH3_1st	e5gzzA2	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: GH3_1st	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)
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)
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)
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)
G	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
G	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
B, C, D, E, F B, C, D, E, F, G	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
B, C, D, E, F B, C, D, E, F, G	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
A	PF03321	GH3 auxin-responsive promoter (GH3)	GH3 auxin-responsive promoter	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B, C, D, E, F B, C, D, E, F, G	Glutathione S-transferase class-mu 26 kDa isozyme	glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	glutathione metabolic process modified amino acid metabolic process metabolic process cellular process sulfur compound metabolic process amide metabolic process	-
A	Jasmonic acid-amido synthetase JAR1	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding acid-amino acid ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity amino acid binding jasmonoyl-L-amino acid ligase activity protein binding enzyme binding cation binding organic acid binding L-leucine binding carboxylic acid binding	response to light stimulus regulation of biological process response to stimulus regulation of response to stimulus biological regulation regulation of response to red or far red light response to radiation response to abiotic stimulus response to red or far red light cellular response to stimulus response to endogenous stimulus cellular response to auxin stimulus response to auxin cellular response to endogenous stimulus response to light stimulus regulation of biological process response to stimulus regulation of response to stimulus biological regulation regulation of response to red or far red light response to radiation response to abiotic stimulus response to red or far red light cellular response to stimulus response to endogenous stimulus cellular response to auxin stimulus response to auxin cellular response to endogenous stimulus cellular response to chemical stimulus response to hormone response to chemical cellular process cellular response to hormone stimulus response to UV response to UV-B response to mycotoxin response to toxic substance positive regulation of response to biotic stimulus regulation of cellular process response to biotic stimulus cell communication induced systemic resistance, jasmonic acid mediated signaling pathway positive regulation of immune response response to bacterium regulation of immune system process signal transduction positive regulation of immune system process immune response response to other organism response to jasmonic acid regulation of innate immune response response to fatty acid response to external stimulus jasmonic acid mediated signaling pathway cellular response to oxygen-containing compound immune effector process cellular response to fatty acid defense response to other organism cellular response to lipid positive regulation of defense response activation of innate immune response regulation of immune response activation of immune response regulation of defense response regulation of response to biotic stimulus biological process involved in interspecies interaction between organisms regulation of response to external stimulus response to lipid signaling positive regulation of biological process hormone-mediated signaling pathway positive regulation of response to stimulus defense response to bacterium positive regulation of response to external stimulus cellular response to jasmonic acid stimulus regulation of response to stress response to stress innate immune response response to external biotic stimulus positive regulation of innate immune response defense response response to oxygen-containing compound defense response to symbiont induced systemic resistance immune system process protein nucleotidylation protein adenylylation macromolecule modification metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, C, D, E, F B, C, D, E, F, G	IPR004046	Glutathione S-transferase, C-terminal	Domain
B, C, D, E, F B, C, D, E, F, G	IPR050213	Glutathione S-transferase superfamily	Family
B, C, D, E, F B, C, D, E, F, G	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
B, C, D, E, F B, C, D, E, F, G	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
B, C, D, E, F B, C, D, E, F, G	IPR004045	Glutathione S-transferase, N-terminal	Domain
B, C, D, E, F B, C, D, E, F, G	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
B, C, D, E, F B, C, D, E, F, G	IPR040079	Glutathione transferase family	Family
A	IPR004993	GH3 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 R01GM157729.