5ECP

Crystal Structure of FIN219-FIP1 complex with JA, MET and ATP

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)
C	d5ecpc2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
C	d5ecpc1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
E	d5ecpe2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
E	d5ecpe1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
F	d5ecpf2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
F	d5ecpf1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d5ecpb2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d5ecpb1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	Mouse-ear 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)
D	GH3_2nd	e5ecpD1	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)
D	GH3_3rd	e5ecpD2	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)
D	GH3_1st	e5ecpD3	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)
A	GH3_2nd	e5ecpA3	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	e5ecpA2	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	e5ecpA1	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)
C	GST_C_3	e5ecpC2	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	e5ecpC1	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	e5ecpE1	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	e5ecpE2	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	e5ecpF1	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	e5ecpF2	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	e5ecpB1	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	e5ecpB2	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)
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)
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)
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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, D	PF03321	GH3 auxin-responsive promoter (GH3)	GH3 auxin-responsive promoter	-	Family
B, C, E, F	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
B, C, 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, D	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	intracellular anatomical structure cytoplasm cellular anatomical entity
B, C, E, F	Glutathione S-transferase U20	amide binding modified amino acid binding binding ion binding oligopeptide binding anion binding glutathione binding sulfur compound binding small molecule binding glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity protein binding amide binding modified amino acid binding binding ion binding oligopeptide binding anion binding glutathione binding sulfur compound binding small molecule binding glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity protein binding enzyme 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 catabolic process detoxification cellular metabolic process response to toxic substance secondary metabolic process 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 catabolic process detoxification cellular metabolic process response to toxic substance secondary metabolic process cellular catabolic process toxin catabolic process response to chemical metabolic process cellular process toxin metabolic process response to gravity glutathione metabolic process sulfur compound metabolic process amide metabolic process cellular modified amino acid metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cytosol extracellular region apoplast plastid chloroplast nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, D	IPR004993	GH3 family	Family
B, C, E, F	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
B, C, E, F	IPR045073	Glutathione S-transferase Omega/Tau-like	Family
B, C, E, F	IPR004045	Glutathione S-transferase, N-terminal	Domain
B, C, E, F	IPR045074	Glutathione S-transferases Tau, C-terminal alpha helical domain, plant	Domain
B, C, E, F	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
B, C, E, F	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
B, C, E, F	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 R01GM157729.