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 | 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 |
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 |