1M0U
Crystal Structure of the Drosophila Glutathione S-transferase-2 in Complex with Glutathione
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0004602 | molecular_function | glutathione peroxidase activity |
| A | 0004667 | molecular_function | prostaglandin-D synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016740 | molecular_function | transferase activity |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0004602 | molecular_function | glutathione peroxidase activity |
| B | 0004667 | molecular_function | prostaglandin-D synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016740 | molecular_function | transferase activity |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | ARG244 |
| B | HOH445 |
| B | HOH452 |
| B | HOH533 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ILE241 |
| A | ARG244 |
| A | HOH560 |
| A | HOH574 |
| A | HOH625 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GSH A 500 |
| Chain | Residue |
| A | TYR54 |
| A | PHE55 |
| A | LEU60 |
| A | TRP85 |
| A | GLN96 |
| A | MET97 |
| A | GLN109 |
| A | SER110 |
| A | HOH522 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 154 |
| Details | Domain: {"description":"GST N-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 244 |
| Details | Domain: {"description":"GST C-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12547198","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| A | TYR54 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| B | TYR54 |
