##gff-version 3 P24473 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1883325;Dbxref=PMID:1883325 P24473 UniProtKB Chain 2 226 . . . ID=PRO_0000185893;Note=Glutathione S-transferase kappa 1 P24473 UniProtKB Binding site 16 18 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14717589;Dbxref=PMID:14717589 P24473 UniProtKB Binding site 53 53 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14717589;Dbxref=PMID:14717589 P24473 UniProtKB Binding site 183 183 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14717589;Dbxref=PMID:14717589 P24473 UniProtKB Binding site 200 201 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14717589;Dbxref=PMID:14717589 P24473 UniProtKB Modified residue 36 36 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 49 49 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 68 68 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 68 68 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 74 74 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 74 74 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 85 85 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 93 93 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 93 93 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 116 116 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 116 116 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 144 144 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 158 158 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 158 158 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 165 165 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 167 167 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 167 167 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 177 177 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 177 177 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Modified residue 193 193 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCM2 P24473 UniProtKB Mutagenesis 16 16 . . . Note=Reduces catalytic activity about 30-fold. Reduces affinity for glutathione about 4-fold. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14717589;Dbxref=PMID:14717589 P24473 UniProtKB Sequence conflict 2 2 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 P24473 UniProtKB Beta strand 6 12 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 17 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Turn 30 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Beta strand 33 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 44 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 60 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 90 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 97 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 111 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 114 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 135 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 149 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Turn 157 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 162 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Beta strand 185 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Beta strand 193 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W P24473 UniProtKB Helix 203 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1R4W