6SJC
Structure of T. thermophilus AspRS in Complex with 5'-O-(N-(L-aspartyl)-sulfamoyl)adenosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004815 | molecular_function | aspartate-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 | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004815 | molecular_function | aspartate-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 | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
| B | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue DSZ A 601 |
| Chain | Residue |
| A | SER199 |
| A | GLN237 |
| A | HIS442 |
| A | HIS443 |
| A | GLU476 |
| A | GLY478 |
| A | GLY479 |
| A | GLY480 |
| A | ARG483 |
| A | ILE525 |
| A | ALA526 |
| A | GLN201 |
| A | GLY528 |
| A | ARG531 |
| A | HOH719 |
| A | HOH765 |
| A | HOH788 |
| A | HOH791 |
| A | LYS204 |
| A | ARG223 |
| A | GLU225 |
| A | ASP230 |
| A | ARG231 |
| A | GLN232 |
| A | PHE235 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue DSZ B 601 |
| Chain | Residue |
| B | GLU177 |
| B | SER199 |
| B | GLN201 |
| B | LYS204 |
| B | ARG223 |
| B | GLU225 |
| B | ASP230 |
| B | ARG231 |
| B | GLN232 |
| B | PHE235 |
| B | GLN237 |
| B | HIS443 |
| B | GLU476 |
| B | VAL477 |
| B | GLY478 |
| B | GLY479 |
| B | GLY480 |
| B | ARG483 |
| B | ILE525 |
| B | ALA526 |
| B | GLY528 |
| B | ARG531 |
| B | HOH745 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00044 |
| Chain | Residue | Details |
| A | GLU177 | |
| B | GLN232 | |
| B | HIS442 | |
| B | GLU476 | |
| B | ARG483 | |
| B | GLY528 | |
| A | ARG223 | |
| A | GLN232 | |
| A | HIS442 | |
| A | GLU476 | |
| A | ARG483 | |
| A | GLY528 | |
| B | GLU177 | |
| B | ARG223 |
