1ATI
CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion 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 | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006426 | biological_process | glycyl-tRNA aminoacylation |
| A | 0009345 | cellular_component | glycine-tRNA ligase complex |
| A | 0016594 | molecular_function | glycine binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion 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 | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006426 | biological_process | glycyl-tRNA aminoacylation |
| B | 0009345 | cellular_component | glycine-tRNA ligase complex |
| B | 0016594 | molecular_function | glycine binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | SA1 |
| Number of Residues | 14 |
| Details | THESE RESIDUES ARE FOUND TO BE RESPONSIBLE FOR ON THE BASIS OF MODELLING GLYCYL-AMP INTO THE ACTIVE SITE OF GLYCYL-TRNA SYNTHETASE. |
| Chain | Residue |
| A | HIS79 |
| A | GLU304 |
| A | ARG311 |
| A | GLU359 |
| A | SER361 |
| A | ARG366 |
| A | GLU188 |
| A | ARG220 |
| A | GLU222 |
| A | PHE235 |
| A | GLN237 |
| A | GLU239 |
| A | GLU241 |
| A | ASP293 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG98 | |
| B | ARG98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU188 | |
| A | PHE235 | |
| A | GLU359 | |
| B | GLU188 | |
| B | PHE235 | |
| B | GLU359 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10064708 |
| Chain | Residue | Details |
| A | ARG220 | |
| A | PHE230 | |
| A | GLU304 | |
| A | GLY363 | |
| B | ARG220 | |
| B | PHE230 | |
| B | GLU304 | |
| B | GLY363 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| A | ARG220 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| B | ARG220 |
