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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Cd5a4vc2 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)
Cd5a4vc1 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)
Dd5a4vd2 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)
Dd5a4vd1 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)
Ed5a4ve2 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)
Ed5a4ve1 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)
Ad5a4va2 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)
Ad5a4va1 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)
Bd5a4vb2 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)
Bd5a4vb1 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)
Fd5a4vf2 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)
Fd5a4vf1 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

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
CSCOP2B SuperfamilyGST C-terminal domain-like8037556 3000305 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyThioredoxin-like8044380 3000031 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyGST C-terminal domain-like8037556 3000305 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyThioredoxin-like8044380 3000031 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyThioredoxin-like8044380 3000031 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyGST C-terminal domain-like8037556 3000305 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThioredoxin-like8044380 3000031 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyGST C-terminal domain-like8037556 3000305 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyGST C-terminal domain-like8037556 3000305 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioredoxin-like8044380 3000031 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyThioredoxin-like8044380 3000031 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyGST C-terminal domain-like8037556 3000305 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
CGST_C_3e5a4vC1 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_Ne5a4vC2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
DGST_C_3e5a4vD1 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_Ne5a4vD2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
EGST_C_3e5a4vE2 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_Ne5a4vE1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
AGST_C_3e5a4vA2 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_Ne5a4vA1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
BGST_C_3e5a4vB1 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_Ne5a4vB2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
FGST_C_3e5a4vF1 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_Ne5a4vF2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF00043Glutathione S-transferase, C-terminal domain (GST_C)Glutathione S-transferase, C-terminal domainGST 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
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 F2

InterPro: Protein Family Classification InterPro Database Homepage