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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Cd1z9hc1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Cd1z9hc2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Ad1z9ha1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Ad1z9ha2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Bd1z9hb1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Bd1z9hb2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Dd1z9hd1 All alpha proteins GST C-terminal domain-like GST C-terminal domain-like Glutathione S-transferase (GST), C-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)
Dd1z9hd2 Alpha and beta proteins (a/b) Thioredoxin fold Thioredoxin-like Glutathione S-transferase (GST), N-terminal domain Microsomal prostaglandin E synthase-2 crab-eating macaque (Macaca fascicularis ) [TaxId: 9541 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
CSCOP2B SuperfamilyThioredoxin-like 8035444 3000031 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyGST C-terminal domain-like 8035442 3000305 SCOP2B (2022-06-29)
ASCOP2 FamilyGlutathione S-transferase (GST), C-terminal domain 8023062 4000976 SCOP2 (2022-06-29)
ASCOP2 FamilyGlutathione S-transferase (GST), N-terminal domain 8023064 4000472 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyGST C-terminal domain-like 8035442 3000305 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyThioredoxin-like 8035444 3000031 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyGST C-terminal domain-like 8035442 3000305 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioredoxin-like 8035444 3000031 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyGST C-terminal domain-like 8035442 3000305 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyThioredoxin-like 8035444 3000031 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
CGST_C_2e1z9hC1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_2ECOD (1.6)
CGlutaredoxine1z9hC2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GlutaredoxinECOD (1.6)
AGST_C_2e1z9hA1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_2ECOD (1.6)
AGlutaredoxine1z9hA2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GlutaredoxinECOD (1.6)
BGST_C_2e1z9hB1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_2ECOD (1.6)
BGlutaredoxine1z9hB2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GlutaredoxinECOD (1.6)
DGST_C_2e1z9hD1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Glutathione S-transferase (GST)-C (From Topology)T: Glutathione S-transferase (GST)-CF: GST_C_2ECOD (1.6)
DGlutaredoxine1z9hD2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: GlutaredoxinECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF13417Glutathione S-transferase, N-terminal domain (GST_N_3)Glutathione S-transferase, N-terminal domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
membrane-associated prostaglandin E synthase-2

Membrane Protein Annotation: OPM OPM Database Homepage

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

ChainsEnzyme NameDescriptionCatalytic Residues
prostaglandin-E synthase  M-CSA #192

Microsomal Prostaglandin E Synthase Type 2 (mPGES-2), sourced from Macaca fascicularis catalyses the isomerization reaction of PGH2 (Prostaglandin H2) to PGE2 (Prostaglandin E2). PGH2 is formed from arachidonic acid. It is an unstable intermediate and so is converted into PGE2. PGE2 exerts control over various biological activities such as relaxation/ contraction of smooth muscle, excretion of Na+, body temperature and the physiological sleep/ wake cycle.

The enzyme is active in the absence of an R-SH reagent, but the catalytic activity is increased by the presence of an R-SH reagent, suggesting that a water molecule and the SH group of an R-SH bind the same site and participate in the same catalytic role. An R-SH or water molecule bound between O-eta of Tyr107 and C9 of PGH2 is polarised by forming a H-bond with Tyr107, and consequently, the SH group of R-SH or water is deprotonated at neutral pH.

Defined by 4 residues: TYR:A-20 [auth A-107]CYS:A-23 [auth A-110]PHE:A-25 [auth A-112]CYS:A-26 [auth A-113]
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