Brand  (β version)

PDB ID: 12GS

Hetero Atom Contents

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain: Hide other chain(s)

Ligands
Code Name Link
0HH L-gamma-glutamyl-S-nonyl-L-cysteinylglycine PoSSuM
MES 2-(N-morpholino)-ethanesulfonic acid PoSSuM

Structure summary

Code : 12GS   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
Release Data : 1999-01-13
Compound :
mol_id molecule chains synonym
1 GLUTATHIONE S-TRANSFERASE A,B GST
ec: 2.5.1.18
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: GSTP1
Authors : Oakley, A.J., Lo Bello, M., Parker, M.W.
Keywords : COMPLEX (TRANSFERASE-NONYL-GLUTATHIONE), TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.10 Å )
Citation :

The Ligandin (Non-Substrate) Binding Site of Human Pi Class Glutathione Transferase is Located in the Electrophile Binding Site (H-Site).

Oakley, A.J.,Lo Bello, M.,Nuccetelli, M.  et al.
(1999)  J.Mol.Biol.  291 : 913

PubMed: 10452896
DOI: 10.1006/jmbi.1999.3029

Reaction

Chain : A, B
UniProt : P09211 (GSTP1_HUMAN)
Reaction : Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:1540159, ECO:0000269|PubMed:1567427, ECO:0000269|PubMed:8433974}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000305};
Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)- glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000269|PubMed:9084911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000305|PubMed:9084911};
Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)- glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133772; Evidence={ECO:0000269|PubMed:9084911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809; Evidence={ECO:0000305|PubMed:9084911};
Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)- glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133769; Evidence={ECO:0000269|PubMed:9084911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801; Evidence={ECO:0000305|PubMed:9084911};
Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)- eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence={ECO:0000269|PubMed:21046276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000305|PubMed:21046276};