1VA6
Crystal structure of Gamma-glutamylcysteine synthetase from Escherichia Coli B complexed with Transition-state analogue
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004357 | molecular_function | glutamate-cysteine ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006750 | biological_process | glutathione biosynthetic process |
| A | 0006972 | biological_process | hyperosmotic response |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071243 | biological_process | cellular response to arsenic-containing substance |
| A | 0071288 | biological_process | cellular response to mercury ion |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004357 | molecular_function | glutamate-cysteine ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006750 | biological_process | glutathione biosynthetic process |
| B | 0006972 | biological_process | hyperosmotic response |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071243 | biological_process | cellular response to arsenic-containing substance |
| B | 0071288 | biological_process | cellular response to mercury ion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 522 |
| Chain | Residue |
| A | GLU29 |
| A | ASP60 |
| A | GLU67 |
| A | P2S520 |
| A | MG524 |
| A | HOH571 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 523 |
| Chain | Residue |
| A | P2S520 |
| A | ADP521 |
| A | MG524 |
| A | GLU27 |
| A | HIS150 |
| A | GLU328 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 524 |
| Chain | Residue |
| A | GLU27 |
| A | GLU67 |
| A | P2S520 |
| A | ADP521 |
| A | MG522 |
| A | MG523 |
| A | HOH705 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 525 |
| Chain | Residue |
| A | ASP408 |
| A | HOH546 |
| A | HOH574 |
| A | HOH696 |
| B | HOH1628 |
| B | HOH1643 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1522 |
| Chain | Residue |
| B | GLU29 |
| B | ASP60 |
| B | GLU67 |
| B | P2S1520 |
| B | MG1524 |
| B | HOH1657 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1523 |
| Chain | Residue |
| B | GLU27 |
| B | HIS150 |
| B | GLU328 |
| B | P2S1520 |
| B | ADP1521 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1524 |
| Chain | Residue |
| B | GLU27 |
| B | GLU67 |
| B | P2S1520 |
| B | ADP1521 |
| B | MG1522 |
| B | HOH1677 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1525 |
| Chain | Residue |
| A | HOH709 |
| B | ASP408 |
| B | HOH1664 |
| B | HOH1666 |
| B | HOH1667 |
| B | HOH1678 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE P2S A 520 |
| Chain | Residue |
| A | GLU27 |
| A | GLU29 |
| A | ASP60 |
| A | GLU67 |
| A | TYR131 |
| A | LEU135 |
| A | GLN144 |
| A | ILE146 |
| A | SER147 |
| A | GLY148 |
| A | HIS150 |
| A | ARG235 |
| A | TYR241 |
| A | TYR300 |
| A | GLU328 |
| A | ARG330 |
| A | ADP521 |
| A | MG522 |
| A | MG523 |
| A | MG524 |
| A | P6G526 |
| A | HOH570 |
| A | HOH584 |
| A | HOH697 |
| A | HOH705 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 521 |
| Chain | Residue |
| A | GLN23 |
| A | GLY25 |
| A | LEU26 |
| A | GLU27 |
| A | GLU67 |
| A | ILE69 |
| A | THR70 |
| A | PRO71 |
| A | VAL72 |
| A | ASN152 |
| A | SER154 |
| A | LYS306 |
| A | GLU325 |
| A | TYR326 |
| A | GLU328 |
| A | P2S520 |
| A | MG523 |
| A | MG524 |
| A | HOH538 |
| A | HOH549 |
| A | HOH564 |
| A | HOH584 |
| A | HOH614 |
| A | HOH683 |
| A | HOH693 |
| A | HOH705 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE P6G A 526 |
| Chain | Residue |
| A | TYR188 |
| A | ARG235 |
| A | LEU236 |
| A | TYR300 |
| A | ARG330 |
| A | LEU370 |
| A | ARG374 |
| A | TRP377 |
| A | P2S520 |
| A | HOH644 |
| A | HOH645 |
| site_id | BC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE P2S B 1520 |
| Chain | Residue |
| B | GLU27 |
| B | GLU29 |
| B | ASP60 |
| B | GLU67 |
| B | TYR131 |
| B | LEU135 |
| B | GLN144 |
| B | ILE146 |
| B | SER147 |
| B | GLY148 |
| B | HIS150 |
| B | ARG235 |
| B | TYR241 |
| B | ASN297 |
| B | TYR300 |
| B | GLU328 |
| B | ARG330 |
| B | ADP1521 |
| B | MG1522 |
| B | MG1523 |
| B | MG1524 |
| B | P6G1526 |
| B | HOH1555 |
| B | HOH1658 |
| B | HOH1677 |
| site_id | BC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP B 1521 |
| Chain | Residue |
| B | GLN23 |
| B | GLY25 |
| B | LEU26 |
| B | GLU27 |
| B | GLU67 |
| B | ILE69 |
| B | THR70 |
| B | PRO71 |
| B | VAL72 |
| B | ASN152 |
| B | PHE153 |
| B | SER154 |
| B | LYS306 |
| B | GLU325 |
| B | TYR326 |
| B | GLU328 |
| B | P2S1520 |
| B | MG1523 |
| B | MG1524 |
| B | HOH1613 |
| B | HOH1655 |
| B | HOH1658 |
| B | HOH1661 |
| B | HOH1677 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE P6G B 1526 |
| Chain | Residue |
| B | TYR188 |
| B | ARG235 |
| B | LEU236 |
| B | TYR300 |
| B | ARG330 |
| B | ARG374 |
| B | TRP377 |
| B | P2S1520 |
| B | HOH1632 |
| B | HOH1633 |
