Annotations: 2PMT

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2pmta1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
A	d2pmta2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
B	d2pmtb1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
B	d2pmtb2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
C	d2pmtc1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
C	d2pmtc2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
D	d2pmtd1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)
D	d2pmtd2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class beta GST	(Proteus mirabilis ) [TaxId: 584 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Thioredoxin-like	8044384	3000031	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GST C-terminal domain-like	8037562	3000305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8044384	3000031	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GST C-terminal domain-like	8037562	3000305	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin-like	8044384	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GST C-terminal domain-like	8037562	3000305	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin-like	8044384	3000031	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	GST C-terminal domain-like	8037562	3000305	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	PF00043	e2pmtA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF00043	ECOD (1.6)
A	PF13409	e2pmtA2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13409	ECOD (1.6)
B	PF00043	e2pmtB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF00043	ECOD (1.6)
B	PF13409	e2pmtB2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13409	ECOD (1.6)
C	PF00043	e2pmtC1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF00043	ECOD (1.6)
C	PF13409	e2pmtC2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13409	ECOD (1.6)
D	PF00043	e2pmtD1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: PF00043	ECOD (1.6)
D	PF13409	e2pmtD2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13409	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	PF13409	Glutathione S-transferase, N-terminal domain (GST_N_2)	Glutathione S-transferase, N-terminal domain	This family is closely related to Pfam:PF02798.	Domain
A, B, C, D	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	GLUTATHIONE TRANSFERASE	glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR004046	Glutathione S-transferase, C-terminal	Domain
A, B, C, D	IPR010987	Glutathione S-transferase, C-terminal-like	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 National Science Foundation (DBI-1832184), 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.