3KAJ
Apoenzyme structure of homoglutathione synthetase from Glycine max in open conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004363 | molecular_function | glutathione synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006750 | biological_process | glutathione biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0043295 | molecular_function | glutathione binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004363 | molecular_function | glutathione synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006750 | biological_process | glutathione biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0043295 | molecular_function | glutathione binding |
| B | 0046872 | molecular_function | metal ion binding |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2hgs |
| Chain | Residue | Details |
| A | ARG475 | |
| A | ARG153 | |
| A | SER176 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2hgs |
| Chain | Residue | Details |
| B | ARG475 | |
| B | ARG153 | |
| B | SER176 |
