1SRY
REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| 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 | 0005737 | cellular_component | cytoplasm |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006434 | biological_process | seryl-tRNA aminoacylation |
| A | 0016260 | biological_process | L-selenocysteine biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070905 | molecular_function | serine binding |
| B | 0000049 | molecular_function | tRNA binding |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0016260 | biological_process | L-selenocysteine biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0070905 | molecular_function | serine binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| A | ASP265 | |
| A | GLU258 | |
| A | SER261 | |
| A | ARG256 | |
| A | ARG271 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| B | ASP265 | |
| B | GLU258 | |
| B | SER261 | |
| B | ARG256 | |
| B | ARG271 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| A | ARG256 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| B | ARG256 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 884 |
| Chain | Residue | Details |
| A | ARG256 | electrostatic stabiliser |
| A | ARG271 | electrostatic stabiliser |
| A | GLU345 | metal ligand |
| A | SER348 | metal ligand |
| A | ARG386 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 884 |
| Chain | Residue | Details |
| B | ARG256 | electrostatic stabiliser |
| B | ARG271 | electrostatic stabiliser |
| B | GLU345 | metal ligand |
| B | SER348 | metal ligand |
| B | ARG386 | electrostatic stabiliser |
