Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0009617 | biological_process | response to bacterium |
| A | 0016740 | molecular_function | transferase activity |
| A | 0035634 | biological_process | response to stilbenoid |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0009617 | biological_process | response to bacterium |
| B | 0016740 | molecular_function | transferase activity |
| B | 0035634 | biological_process | response to stilbenoid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GBX A 230 |
| Chain | Residue |
| A | TYR8 |
| A | LEU207 |
| A | ALA215 |
| A | PHE221 |
| A | HOH695 |
| A | HOH845 |
| B | ASP400 |
| B | ARG430 |
| B | HOH651 |
| A | PHE9 |
| A | LYS44 |
| A | ASP52 |
| A | GLN53 |
| A | VAL54 |
| A | GLN66 |
| A | THR67 |
| A | LEU110 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GBX B 530 |
| Chain | Residue |
| A | ASP100 |
| A | ARG130 |
| A | HOH638 |
| A | HOH852 |
| B | PHE309 |
| B | LYS344 |
| B | GLN353 |
| B | VAL354 |
| B | PRO355 |
| B | GLN366 |
| B | THR367 |
| B | LEU507 |
| B | ILE512 |
| B | ALA515 |
| B | ARG516 |
| B | PHE521 |
| B | HOH681 |
| B | HOH823 |
| B | HOH833 |
| B | HOH844 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IPA A 235 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IPA B 236 |
| Chain | Residue |
| B | THR376 |
| B | ASP379 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Domain: {"description":"GST N-terminal"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13745","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12549910","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P30115","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| B | TYR308 | |
