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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1gtia1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Ad1gtia2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Bd1gtib1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Bd1gtib2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Cd1gtic1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Cd1gtic2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Dd1gtid1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Dd1gtid2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Ed1gtie1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Ed1gtie2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Fd1gtif1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)
Fd1gtif2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class pi GST (Mus musculus ) [TaxId: 10090 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyThioredoxin-like8044373 3000031 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyGST C-terminal domain-like8037507 3000305 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioredoxin-like8044373 3000031 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyGST C-terminal domain-like8037507 3000305 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyGST C-terminal domain-like8037507 3000305 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyThioredoxin-like8044373 3000031 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyThioredoxin-like8044373 3000031 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyGST C-terminal domain-like8037507 3000305 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyGST C-terminal domain-like8037507 3000305 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyThioredoxin-like8044373 3000031 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyGST C-terminal domain-like8037507 3000305 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyThioredoxin-like8044373 3000031 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGST_C_3e1gtiA1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
AGST_N_5e1gtiA2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
BGST_C_3e1gtiB1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
BGST_N_5e1gtiB2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
CGST_C_3e1gtiC1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
CGST_N_5e1gtiC2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
DGST_C_3e1gtiD1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
DGST_N_5e1gtiD2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
EGST_C_3e1gtiE1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
EGST_N_5e1gtiE2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
FGST_C_3e1gtiF1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
FGST_N_5e1gtiF2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF14497Glutathione S-transferase, C-terminal domain (GST_C_3)Glutathione S-transferase, C-terminal domainThis domain is closely related to Pfam:PF00043.Domain
A, B, C, D, E
PF02798Glutathione S-transferase, N-terminal domain (GST_N)Glutathione S-transferase, N-terminal domainFunction: 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

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
GLUTATHIONE S-TRANSFERASE

InterPro: Protein Family Classification InterPro Database Homepage