Brand  (β version)

PDB ID: 1GTI

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Ligands
Code Name Style Show Link
GTB S-(P-nitrobenzyl)glutathione PoSSuM
Non-standard Residues
Code Name Show
CCS Carboxymethylated cysteine
Glycosylation
Code Name Emphasize
Modification
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Structure summary

Code : 1GTI   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : MODIFIED GLUTATHIONE S-TRANSFERASE (PI) COMPLEXED WITH S (P-NITROBENZYL)GLUTATHIONE
Release Data : 1999-03-02
Compound :
mol_id molecule chains synonym
1 GLUTATHIONE S-TRANSFERASE A,B,C,D,E,F GST
ec: 2.5.1.18
other_details: CARBOXYMETHYLATION IN RESIDUE CYS 47
Source :
mol_id organism_scientific organism_common
1 Mus musculus  (taxid:10090) House mouse
organ: LIVER
cellular_location: CYTOPLASM
Authors : Vega, M.C., Coll, M.
Keywords : GLUTATHIONE, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 3.0 Å )
Citation :

The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region.

Vega, M.C.,Walsh, S.B.,Mantle, T.J.  et al.
(1998)  J.Biol.Chem.  273 : 2844 - 2850

PubMed: 9446594
DOI: 10.1074/jbc.273.5.2844

Molecular Structure at 1.8 A of Mouse Liver Class Pi Glutathione S-Transferase Complexed with S-(P-Nitrobenzyl)Glutathione and Other Inhibitors

Garcia-Saez, I.,Parraga, A.,Phillips, M.F.  et al.
(1994)  J.Mol.Biol.  237 : 298

Reaction

Chain : A, B, C, D, E, F
UniProt : P19157 (GSTP1_MOUSE)
Reaction: EC: Evidence:
Physiological Direction:
glutathione + RX = a halide anion + an S-substituted glutathione + H(+) 2.5.1.18 UniProtKB:P09211
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glutathione + prostaglandin J2 = prostaglandin J2-S-(R)- glutathione - UniProtKB:P09211
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glutathione + prostaglandin J2 = prostaglandin J2-S-(S)- glutathione - UniProtKB:P09211
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glutathione + prostaglandin A2 = prostaglandin A2-S-(S)- glutathione - UniProtKB:P09211
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11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)- eicosatrienoate - UniProtKB:P09211
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