GSTP1

10GS, 11GS, 12GS, 13GS, 14GS, 16GS, 17GS, 18GS, 19GS, 1AQV, 1AQW, 1AQX, 1EOG, 1EOH, 1GSS, 1KBN, 1LBK, 1MD3, 1MD4, 1PGT, 1PX6, 1PX7, 1ZGN, 20GS, 22GS, 2A2R, 2A2S, 2GSS, 2J9H, 2PGT, 3CSH, 3CSI, 3CSJ, 3DD3, 3DGQ, 3GSS, 3GUS, 3HJM, 3HJO, 3HKR, 3IE3, 3KM6, 3KMN, 3KMO, 3N9J, 3PGT, 4GSS, 4PGT, 5GSS, 6GSS, 7GSS, 8GSS, 9GSS2950100042625ENSG00000084207n/aP09211n/aNM_000852n/aNP_000843n/aGlutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.10gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER11711gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE (FORM II)12gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE13gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE14gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 116gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 317gs: GLUTATHIONE S-TRANSFERASE P1-118gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE19gs: GLUTATHIONE S-TRANSFERASE P1-11aqv: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE1aqw: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE1aqx: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX1eog: CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE1eoh: GLUTATHIONE TRANSFERASE P1-11gss: THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION1kbn: Glutathione transferase mutant1lbk: Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme1md3: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to alanine1md4: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine1pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH S-HEXYLGLUTATHIONE1px6: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine1px7: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate1zgn: Crystal Structure of the Glutathione Transferase Pi in Complex with Dinitrosyl-diglutathionyl Iron Complex20gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE21gs:22gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT2a2r: Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione2a2s: Crystal Structure of Human Glutathione Transferase in complex with S-nitrosoglutathione in the absence of reducing agent2gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID2j9h: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE-S-TRANSFERASE P1-1 CYS-FREE MUTANT IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.4 A RESOLUTION2pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE3gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE3pgt: CRYSTAL STRUCTURE OF HGSTP1-1 COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE4gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT4pgt: CRYSTAL STRUCTURE OF HGSTP1-1 COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE5gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE6gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE7gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE8gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE9gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH S-HEXYL GLUTATHIONE Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene. Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into four main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases. GSTP1 has been shown to interact with Fanconi anemia, complementation group C and MAPK8. GST-Pi is expressed in many human tissues, particularly in the biliary tree, renal distal convoluted tubules and lungs. Triple-negative breast cancer cells rely on glutathione-S-transferase Pi1, and inhibitors are being studied. Piperlongumine has been found to silence the gene.