Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGST C-terminal domain-like 8036511 3000305 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThioredoxin-like 8036512 3000031 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioredoxin-like 8036512 3000031 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyGST C-terminal domain-like 8036511 3000305 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGST_C_3e18gsA1 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_5e18gsA2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
BGST_C_3e18gsB1 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_5e18gsB2 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
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
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
GLUTATHIONE S-TRANSFERASE

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B
PharosP09211