5I9K
The structure of microsomal glutathione transferase 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0004602 | molecular_function | glutathione peroxidase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005741 | cellular_component | mitochondrial outer membrane |
A | 0005778 | cellular_component | peroxisomal membrane |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0016020 | cellular_component | membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0032496 | biological_process | response to lipopolysaccharide |
A | 0033327 | biological_process | Leydig cell differentiation |
A | 0034635 | biological_process | glutathione transport |
A | 0042802 | molecular_function | identical protein binding |
A | 0043295 | molecular_function | glutathione binding |
A | 0045177 | cellular_component | apical part of cell |
A | 0071449 | biological_process | cellular response to lipid hydroperoxide |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue GSH A 201 |
Chain | Residue |
A | ARG38 |
A | HIS76 |
A | LEU77 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PC1 A 202 |
Chain | Residue |
A | ILE105 |
A | VAL136 |
A | VAL140 |
A | MET144 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue PC1 A 203 |
Chain | Residue |
A | PRO124 |
A | TYR116 |
A | ALA120 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PLM A 204 |
Chain | Residue |
A | LEU30 |
A | ILE115 |
A | THR118 |
A | ILE119 |
A | TYR121 |
A | LEU122 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue PLM A 205 |
Chain | Residue |
A | PRO85 |
A | ILE89 |
A | LEU92 |
A | TYR93 |
A | LEU149 |
A | LEU153 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:16806268 |
Chain | Residue | Details |
A | ASP3-ASP9 | |
A | GLY97-ASP99 | |
A | LEU149-LEU155 |
site_id | SWS_FT_FI2 |
Number of Residues | 98 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | ASN10-ALA33 | |
A | LEU63-SER96 | |
A | LEU100-THR123 | |
A | ASN129-LEU148 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16806268 |
Chain | Residue | Details |
A | THR34-PHE62 | |
A | PRO124-PRO128 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16806268 |
Chain | Residue | Details |
A | ARG38 | |
A | ARG73 | |
A | ARG74 | |
A | HIS76 | |
A | GLU81 | |
A | TYR121 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Activates the enzyme when modified in vitro => ECO:0000269|PubMed:11106493 |
Chain | Residue | Details |
A | CYS50 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91VS7 |
Chain | Residue | Details |
A | LYS42 | |
A | LYS55 | |
A | LYS60 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: 3'-nitrotyrosine; in vitro => ECO:0000269|PubMed:16314419 |
Chain | Residue | Details |
A | TYR93 |