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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1xw6a1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ad1xw6a2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd1xw6b1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd1xw6b2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd1xw6c1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd1xw6c2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Dd1xw6d1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Dd1xw6d2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Class mu GST human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGST_C_3e1xw6A1 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_5e1xw6A2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
BGST_C_3e1xw6B1 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_5e1xw6B2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
CGST_C_3e1xw6C1 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_5e1xw6C2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GST_N_5ECOD (1.6)
DGST_C_3e1xw6D1 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_5e1xw6D2 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
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
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
Glutathione S-transferase Mu 1

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
Glutathione S-transferase class-μ  M-CSA #867

Glutathione S-transferases (GSTs) are promiscuous enzymes that catalyze several reactions with various substrates. Their essential function is detoxification of xenobiotic compounds that are conjugated to glutathione (GSH) and then excreted; other functions, not associated with detoxification, include repair of macromolecules oxidised by reactive oxygen species, regeneration of S-thiolated proteins, and biosynthesis of physiologically important metabolites. There are two proposed mechanisms regarding GSH activation depending on the conformation of Tyr10 (in and out). Both appear to be viable where evidence supports both conformations.

Defined by 3 residues: TYR:A-7 [auth A-6]ARG:A-43 [auth A-42]HIS:A-108 [auth A-107]
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