1R4W
Crystal structure of Mitochondrial class kappa glutathione transferase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0004602 | molecular_function | glutathione peroxidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005777 | cellular_component | peroxisome |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0004602 | molecular_function | glutathione peroxidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005777 | cellular_component | peroxisome |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0030855 | biological_process | epithelial cell differentiation |
B | 0098869 | biological_process | cellular oxidant detoxification |
C | 0004364 | molecular_function | glutathione transferase activity |
C | 0004602 | molecular_function | glutathione peroxidase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005777 | cellular_component | peroxisome |
C | 0006749 | biological_process | glutathione metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016740 | molecular_function | transferase activity |
C | 0030855 | biological_process | epithelial cell differentiation |
C | 0098869 | biological_process | cellular oxidant detoxification |
D | 0004364 | molecular_function | glutathione transferase activity |
D | 0004602 | molecular_function | glutathione peroxidase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005777 | cellular_component | peroxisome |
D | 0006749 | biological_process | glutathione metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016740 | molecular_function | transferase activity |
D | 0030855 | biological_process | epithelial cell differentiation |
D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GSH A 301 |
Chain | Residue |
A | SER16 |
A | SER200 |
A | ASP201 |
B | LYS62 |
B | ARG202 |
A | PRO17 |
A | TYR18 |
A | ASN53 |
A | PHE181 |
A | GLY182 |
A | LEU183 |
A | PHE198 |
A | GLY199 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GSH B 401 |
Chain | Residue |
A | LYS62 |
A | ARG202 |
B | SER16 |
B | PRO17 |
B | TYR18 |
B | LEU44 |
B | MET48 |
B | ASN53 |
B | GLY182 |
B | LEU183 |
B | PHE198 |
B | GLY199 |
B | SER200 |
B | ASP201 |
B | HOH560 |
B | HOH669 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GSH C 801 |
Chain | Residue |
C | SER16 |
C | PRO17 |
C | TYR18 |
C | GLY182 |
C | LEU183 |
C | SER200 |
C | ASP201 |
C | HOH765 |
D | LYS62 |
D | ARG202 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GSH D 901 |
Chain | Residue |
C | LYS62 |
C | ARG202 |
D | SER16 |
D | PRO17 |
D | TYR18 |
D | MET48 |
D | PHE181 |
D | GLY182 |
D | LEU183 |
D | PHE198 |
D | GLY199 |
D | SER200 |
D | ASP201 |
D | HOH763 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14717589 |
Chain | Residue | Details |
A | PRO17 | |
C | GLN54 | |
C | PRO184 | |
C | ASP201 | |
D | PRO17 | |
D | GLN54 | |
D | PRO184 | |
D | ASP201 | |
A | GLN54 | |
A | PRO184 | |
A | ASP201 | |
B | PRO17 | |
B | GLN54 | |
B | PRO184 | |
B | ASP201 | |
C | PRO17 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DCM2 |
Chain | Residue | Details |
A | LEU37 | |
C | ASP50 | |
C | ALA145 | |
C | THR194 | |
D | LEU37 | |
D | ASP50 | |
D | ALA145 | |
D | THR194 | |
A | ASP50 | |
A | ALA145 | |
A | THR194 | |
B | LEU37 | |
B | ASP50 | |
B | ALA145 | |
B | THR194 | |
C | LEU37 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCM2 |
Chain | Residue | Details |
A | GLU69 | |
B | LYS94 | |
B | VAL117 | |
B | ILE159 | |
B | LEU168 | |
B | TYR178 | |
C | GLU69 | |
C | GLN75 | |
C | LYS94 | |
C | VAL117 | |
C | ILE159 | |
A | GLN75 | |
C | LEU168 | |
C | TYR178 | |
D | GLU69 | |
D | GLN75 | |
D | LYS94 | |
D | VAL117 | |
D | ILE159 | |
D | LEU168 | |
D | TYR178 | |
A | LYS94 | |
A | VAL117 | |
A | ILE159 | |
A | LEU168 | |
A | TYR178 | |
B | GLU69 | |
B | GLN75 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCM2 |
Chain | Residue | Details |
A | ASP86 | |
A | SER166 | |
B | ASP86 | |
B | SER166 | |
C | ASP86 | |
C | SER166 | |
D | ASP86 | |
D | SER166 |