Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0004825 | molecular_function | methionine-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006412 | biological_process | translation |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 0006431 | biological_process | methionyl-tRNA aminoacylation |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue ME8 C 601 |
Chain | Residue |
C | ALA9 |
C | TRP228 |
C | ALA231 |
C | TYR235 |
C | GLY261 |
C | ASP263 |
C | ILE264 |
C | HIS290 |
C | GLY291 |
C | PHE292 |
C | LEU293 |
C | ILE10 |
C | HOH721 |
C | HOH762 |
C | HOH811 |
C | ALA11 |
C | TYR12 |
C | HIS18 |
C | GLY20 |
C | HIS21 |
C | GLU24 |
C | ASP49 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO C 602 |
Chain | Residue |
C | ARG33 |
C | ASN85 |
C | HOH789 |
C | HOH816 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue MG C 603 |
Chain | Residue |
C | VAL19 |
C | SER301 |
C | VAL308 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue MG C 604 |
Chain | Residue |
C | ARG397 |
C | HOH788 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MG C 605 |
Chain | Residue |
C | TYR23 |
C | LEU326 |
C | VAL330 |
C | PHE332 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MG C 606 |
Chain | Residue |
C | ARG328 |
C | HOH751 |
C | HOH855 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue MG C 607 |
Functional Information from PROSITE/UniProt
site_id | PS00178 |
Number of Residues | 10 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..NAaPHVGHA |
Chain | Residue | Details |
C | PRO13-ALA22 | |