4JFA
Crystal Structure of Plasmodium falciparum Tryptophanyl-tRNA synthetase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TRP A 701 |
| Chain | Residue |
| A | TYR306 |
| A | GLN456 |
| A | PHE460 |
| A | HOH808 |
| A | HOH835 |
| A | HOH852 |
| A | HOH854 |
| A | GLY308 |
| A | ARG309 |
| A | GLY310 |
| A | GLN341 |
| A | GLU346 |
| A | LYS347 |
| A | TYR425 |
| A | GLN429 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 702 |
| Chain | Residue |
| A | CYS256 |
| A | ILE454 |
| A | ASP457 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRP B 701 |
| Chain | Residue |
| B | TYR306 |
| B | GLY308 |
| B | GLY310 |
| B | GLN341 |
| B | GLU346 |
| B | LYS347 |
| B | TYR425 |
| B | GLN429 |
| B | GLN456 |
| B | PHE460 |
| B | HOH823 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 702 |
| Chain | Residue |
| B | CYS256 |
| B | ILE454 |
| B | ASP457 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRP C 701 |
| Chain | Residue |
| C | TYR306 |
| C | GLY308 |
| C | GLY310 |
| C | GLN341 |
| C | GLU346 |
| C | LYS347 |
| C | GLN429 |
| C | GLN456 |
| C | PHE460 |
| C | HOH839 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K C 702 |
| Chain | Residue |
| A | HOH803 |
| C | TYR348 |
| C | HOH801 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TRP D 701 |
| Chain | Residue |
| D | TYR306 |
| D | GLY308 |
| D | ARG309 |
| D | GLY310 |
| D | GLN341 |
| D | SER343 |
| D | GLU346 |
| D | LYS347 |
| D | TYR425 |
| D | GLN429 |
| D | GLN456 |
| D | PHE460 |
| D | HOH806 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME D 702 |
| Chain | Residue |
| D | PHE254 |
| D | CYS256 |
| D | ILE454 |
| D | ASP457 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 703 |
| Chain | Residue |
| B | HOH863 |
| B | HOH864 |
| D | TYR348 |
| D | HOH810 |
