Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0006751 | biological_process | glutathione catabolic process |
| B | 0036374 | molecular_function | glutathione hydrolase activity |
| D | 0006751 | biological_process | glutathione catabolic process |
| D | 0036374 | molecular_function | glutathione hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GLY B 701 |
| Chain | Residue |
| A | ARG94 |
| B | ASN384 |
| B | GLU403 |
| B | ASP406 |
| B | SER435 |
| B | SER436 |
| B | HOH843 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GLY B 702 |
| Chain | Residue |
| B | TRP525 |
| B | GLY703 |
| B | TRP385 |
| B | ASP386 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GLY B 703 |
| Chain | Residue |
| B | THR364 |
| B | ASN384 |
| B | PHE417 |
| B | PRO455 |
| B | GLY456 |
| B | GLY457 |
| B | GLY702 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 704 |
| Chain | Residue |
| A | TRP257 |
| A | ILE279 |
| B | PHE465 |
| B | ASN469 |
| B | TYR472 |
| B | ASP473 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 601 |
| Chain | Residue |
| C | TRP257 |
| C | ILE279 |
| D | PHE465 |
| D | ASN469 |
| D | TYR472 |
| D | ASP473 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GLY D 602 |
| Chain | Residue |
| C | ARG94 |
| D | ASN384 |
| D | GLU403 |
| D | ASP406 |
| D | SER435 |
| D | SER436 |
| D | MET437 |
| D | HOH728 |
Functional Information from PROSITE/UniProt
| site_id | PS00462 |
| Number of Residues | 25 |
| Details | G_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHfSIvdkdGNaVSnTyTLNwdFG |
| Chain | Residue | Details |
| B | THR364-GLY388 | |
