6AA0
Crystal Structure of Toxoplasma gondii Prolyl tRNA Synthetase (TgPRS) in Apo Form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004827 | molecular_function | proline-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006433 | biological_process | prolyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004827 | molecular_function | proline-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006433 | biological_process | prolyl-tRNA aminoacylation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004827 | molecular_function | proline-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006433 | biological_process | prolyl-tRNA aminoacylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004827 | molecular_function | proline-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006433 | biological_process | prolyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 901 |
| Chain | Residue |
| A | GLU516 |
| A | VAL523 |
| A | LYS729 |
| A | LEU732 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 902 |
| Chain | Residue |
| A | GLU497 |
| A | TRP501 |
| A | LYS539 |
| A | LEU561 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 901 |
| Chain | Residue |
| B | ARG614 |
| B | GLN721 |
| B | GLU516 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 902 |
| Chain | Residue |
| B | GLU516 |
| B | VAL523 |
| B | LYS729 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 903 |
| Chain | Residue |
| B | GLU441 |
| B | PHE534 |
| B | HIS560 |
| B | SER588 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 904 |
| Chain | Residue |
| B | GLU497 |
| B | TRP501 |
| B | LYS539 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 901 |
| Chain | Residue |
| C | GLU516 |
| C | PRO522 |
| C | VAL523 |
| C | LYS729 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 902 |
| Chain | Residue |
| A | TYR358 |
| A | TYR359 |
| A | ASP360 |
| A | ILE361 |
| C | TYR358 |
| C | TYR359 |
| C | ASP360 |
| C | ILE361 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 903 |
| Chain | Residue |
| C | GLN619 |
| C | ASP650 |
| C | LEU714 |
| C | MET717 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue GOL D 902 |
| Chain | Residue |
| D | LEU505 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL D 903 |
| Chain | Residue |
| D | GLU497 |
| D | LYS539 |
