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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad4zbba2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
Ad4zbba1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
B [auth C]d4zbbc2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
B [auth C]d4zbbc1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
C [auth B]d4zbbb2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
C [auth B]d4zbbb1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
Dd4zbbd2 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)
Dd4zbbd1 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like automated matches automated matches (Phanerodontia chrysosporium ) [TaxId: 2822231 ], SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGST_C_3e4zbbA2 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_Ne4zbbA1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
B [auth C]GST_C_3e4zbbC1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
B [auth C]GST_Ne4zbbC2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
C [auth B]GST_C_3e4zbbB2 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_3ECOD (1.6)
C [auth B]GST_Ne4zbbB1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_NECOD (1.6)
DGST_C_3e4zbbD1 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_Ne4zbbD2 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 [auth C],
C [auth B],
D
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 [auth C],
C [auth B],
D
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