3RGL
The crystal structure of glycyl-tRNA synthetase subunit alpha from Campylobacter jejuni subsp. jejuni NCTC in complex with ATP and glycine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004820 | molecular_function | glycine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006412 | biological_process | translation |
A | 0006426 | biological_process | glycyl-tRNA aminoacylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004820 | molecular_function | glycine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006412 | biological_process | translation |
B | 0006426 | biological_process | glycyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GLY A 301 |
Chain | Residue |
A | ALA31 |
A | GLY32 |
A | THR33 |
A | ARG58 |
A | GLN76 |
A | GLN78 |
A | THR158 |
A | ATP401 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ATP A 401 |
Chain | Residue |
A | ASP61 |
A | ASN69 |
A | ARG70 |
A | LEU71 |
A | TYR74 |
A | GLN76 |
A | MSE134 |
A | GLU135 |
A | VAL136 |
A | THR137 |
A | GLN138 |
A | THR158 |
A | GLY160 |
A | GLY301 |
A | ARG58 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ATP B 401 |
Chain | Residue |
B | ARG58 |
B | ASP61 |
B | ASN69 |
B | LEU71 |
B | TYR74 |
B | GLU128 |
B | GLU135 |
B | VAL136 |
B | THR137 |
B | GLN138 |
B | THR158 |
B | GLY160 |
B | ARG163 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LMR B 501 |
Chain | Residue |
B | SER117 |
B | PRO118 |
B | SER119 |
B | MSE265 |