6BLJ
Crystal structure of cytoplasmic Serine-tRNA ligase from Naegleria fowleri in complex with AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004828 | molecular_function | serine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006434 | biological_process | seryl-tRNA aminoacylation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004828 | molecular_function | serine-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006434 | biological_process | seryl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue AMP A 500 |
| Chain | Residue |
| A | ARG306 |
| A | SER401 |
| A | THR436 |
| A | ALA439 |
| A | ARG442 |
| A | HOH602 |
| A | HOH641 |
| A | HOH702 |
| A | HOH737 |
| A | HOH766 |
| A | GLU308 |
| A | PHE320 |
| A | ARG321 |
| A | VAL322 |
| A | PHE325 |
| A | GLU398 |
| A | LEU399 |
| A | VAL400 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | ASP346 |
| A | LYS379 |
| A | HOH686 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue AMP B 500 |
| Chain | Residue |
| B | ARG306 |
| B | GLU308 |
| B | PHE320 |
| B | ARG321 |
| B | VAL322 |
| B | PHE325 |
| B | GLU398 |
| B | LEU399 |
| B | VAL400 |
| B | SER401 |
| B | THR436 |
| B | ALA439 |
| B | ARG442 |
| B | HOH607 |
| B | HOH620 |
| B | HOH795 |
| B | HOH868 |
| B | HOH935 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | HIS147 |
| B | TRP342 |
| B | PHE345 |
| B | ASP346 |
| B | LYS379 |
| B | HOH800 |
| B | HOH866 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue AMP C 500 |
| Chain | Residue |
| C | ARG306 |
| C | GLU308 |
| C | PHE320 |
| C | ARG321 |
| C | VAL322 |
| C | PHE325 |
| C | GLU398 |
| C | LEU399 |
| C | VAL400 |
| C | SER401 |
| C | THR436 |
| C | ALA439 |
| C | ARG442 |
| C | HOH604 |
| C | HOH605 |
| C | HOH630 |
| C | HOH718 |
| C | HOH784 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 501 |
| Chain | Residue |
| C | ASP346 |
| C | LYS379 |
| C | HOH684 |
