3KAL
Structure of homoglutathione synthetase from Glycine max in closed conformation with homoglutathione, ADP, a sulfate ion, and three magnesium ions 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 | 25 |
| Details | BINDING SITE FOR RESIDUE ADP A 500 |
| Chain | Residue |
| A | ILE168 |
| A | TYR399 |
| A | MET424 |
| A | GLN425 |
| A | ARG426 |
| A | ILE427 |
| A | GLU450 |
| A | LYS477 |
| A | MG502 |
| A | MG503 |
| A | SO4505 |
| A | GLU169 |
| A | HOH588 |
| A | HOH650 |
| A | HOH683 |
| A | HOH710 |
| A | HOH734 |
| A | HOH864 |
| A | LYS334 |
| A | VAL386 |
| A | LYS388 |
| A | GLU392 |
| A | GLY393 |
| A | GLY394 |
| A | ASN397 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HGS A 501 |
| Chain | Residue |
| A | ARG153 |
| A | ASN171 |
| A | ILE173 |
| A | SER174 |
| A | THR175 |
| A | SER176 |
| A | PHE177 |
| A | GLN238 |
| A | GLU241 |
| A | ASN243 |
| A | ARG295 |
| A | TYR298 |
| A | ARG475 |
| A | VAL486 |
| A | LEU487 |
| A | SO4505 |
| A | HOH688 |
| A | HOH835 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | GLU169 |
| A | ASN171 |
| A | GLU392 |
| A | ADP500 |
| A | SO4505 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | GLU169 |
| A | ADP500 |
| A | SO4505 |
| A | HOH588 |
| A | HOH710 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | GLU169 |
| A | MET170 |
| A | GLY332 |
| A | GLU392 |
| A | HOH566 |
| A | HOH634 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ARG153 |
| A | ASP155 |
| A | GLU169 |
| A | ASN171 |
| A | GLU392 |
| A | GLY393 |
| A | ARG475 |
| A | ADP500 |
| A | HGS501 |
| A | MG502 |
| A | MG503 |
| A | HOH588 |
| A | HOH710 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HGS A 506 |
| Chain | Residue |
| A | TRP49 |
| A | ASN53 |
| A | CYS182 |
| A | LEU183 |
| A | GLY186 |
| A | ASN209 |
| A | ASN210 |
| A | VAL212 |
| A | ASP213 |
| A | HOH658 |
| A | HOH675 |
| A | HOH747 |
| A | HOH828 |
| A | HOH854 |
| A | HOH861 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP B 500 |
| Chain | Residue |
| B | MET424 |
| B | GLN425 |
| B | ARG426 |
| B | ILE427 |
| B | GLU450 |
| B | LYS477 |
| B | MG502 |
| B | MG503 |
| B | SO4505 |
| B | HOH627 |
| B | HOH663 |
| B | HOH684 |
| B | HOH758 |
| B | HOH800 |
| B | ILE168 |
| B | GLU169 |
| B | LYS334 |
| B | VAL386 |
| B | LYS388 |
| B | ARG391 |
| B | GLU392 |
| B | GLY393 |
| B | GLY394 |
| B | ASN396 |
| B | ASN397 |
| B | TYR399 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HGS B 501 |
| Chain | Residue |
| B | ARG153 |
| B | ASN171 |
| B | ILE173 |
| B | SER174 |
| B | THR175 |
| B | SER176 |
| B | GLN238 |
| B | GLU241 |
| B | ASN243 |
| B | ARG295 |
| B | TYR298 |
| B | ARG475 |
| B | GLY485 |
| B | VAL486 |
| B | SO4505 |
| B | HOH545 |
| B | HOH551 |
| B | HOH688 |
| B | HOH807 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | GLU169 |
| B | ASN171 |
| B | GLU392 |
| B | ADP500 |
| B | SO4505 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 503 |
| Chain | Residue |
| B | GLU169 |
| B | ADP500 |
| B | SO4505 |
| B | HOH627 |
| B | HOH663 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 504 |
| Chain | Residue |
| B | GLU169 |
| B | MET170 |
| B | GLY332 |
| B | GLU392 |
| B | HOH537 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SO4 B 505 |
| Chain | Residue |
| B | ARG153 |
| B | ASP155 |
| B | GLU169 |
| B | ASN171 |
| B | GLU392 |
| B | GLY393 |
| B | ARG475 |
| B | ADP500 |
| B | HGS501 |
| B | MG502 |
| B | MG503 |
| B | HOH627 |
| B | HOH663 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HGS B 506 |
| Chain | Residue |
| B | ASN53 |
| B | CYS182 |
| B | LEU183 |
| B | ASP213 |
| B | HOH536 |
| B | HOH655 |
| B | HOH828 |
| B | HOH834 |
