Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004363 | molecular_function | glutathione synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006750 | biological_process | glutathione biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 319 |
| Chain | Residue |
| A | ASP273 |
| A | GLU281 |
| A | ADP317 |
| A | MG320 |
| A | SO4400 |
| A | HOH458 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 320 |
| Chain | Residue |
| A | MG319 |
| A | SO4400 |
| A | HOH513 |
| A | GLU281 |
| A | ASN283 |
| A | ADP317 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | MET165 |
| A | GLY166 |
| A | ARG210 |
| A | ARG225 |
| A | ASN235 |
| A | ASP273 |
| A | GLU281 |
| A | ASN283 |
| A | ADP317 |
| A | GSH318 |
| A | MG319 |
| A | MG320 |
| A | HOH458 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ADP A 317 |
| Chain | Residue |
| A | LYS125 |
| A | ILE158 |
| A | LYS160 |
| A | GLY164 |
| A | MET165 |
| A | GLY166 |
| A | GLY167 |
| A | ILE170 |
| A | GLN198 |
| A | ASN199 |
| A | TYR200 |
| A | LEU201 |
| A | ILE204 |
| A | ASP208 |
| A | THR232 |
| A | ARG233 |
| A | GLY234 |
| A | ASN235 |
| A | ASP273 |
| A | GLU281 |
| A | MG319 |
| A | MG320 |
| A | SO4400 |
| A | HOH445 |
| A | HOH458 |
| A | HOH489 |
| A | HOH513 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GSH A 318 |
| Chain | Residue |
| A | ASP19 |
| A | SER20 |
| A | SER21 |
| A | ARG86 |
| A | ASP88 |
| A | PRO89 |
| A | ARG210 |
| A | ARG225 |
| A | LEU236 |
| A | ALA237 |
| A | THR285 |
| A | SER286 |
| A | PRO287 |
| A | THR288 |
| A | SO4400 |
| A | HOH403 |
| A | HOH511 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP151 | |
| A | GLU281 | |
| A | ASN283 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 8810901 |
| Chain | Residue | Details |
| A | ARG225 | |
| A | LYS160 | |
| A | ARG210 | |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 199 |
| Chain | Residue | Details |
| A | LYS125 | electrostatic stabiliser |
| A | LYS160 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG210 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG225 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG233 | electrostatic stabiliser |
| A | ASP273 | metal ligand |
| A | GLU281 | metal ligand |
| A | ASN283 | metal ligand |
