3KAK
Structure of homoglutathione synthetase from Glycine max in open conformation with gamma-glutamyl-cysteine bound.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004363 | molecular_function | glutathione synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004363 | molecular_function | glutathione synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3GC A 501 |
| Chain | Residue |
| A | ARG153 |
| A | TYR298 |
| A | ILE173 |
| A | SER174 |
| A | THR175 |
| A | SER176 |
| A | GLN238 |
| A | GLU241 |
| A | ASN243 |
| A | ARG295 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 3GC B 501 |
| Chain | Residue |
| B | ARG153 |
| B | SER174 |
| B | SER176 |
| B | GLN238 |
| B | GLU241 |
| B | ASN243 |
| B | ARG295 |
| B | TYR298 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 3GC B 502 |
| Chain | Residue |
| B | TRP90 |
| B | LYS91 |
| B | CYS94 |
| B | PRO207 |
| B | ALA208 |
| B | GLU469 |
