1G51
ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION
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 | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| B | ARG1231 |
| B | ARG1531 |
| B | HOH2391 |
| B | HOH2513 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1901 |
| Chain | Residue |
| A | ARG231 |
| A | ARG531 |
| A | HOH2412 |
| A | HOH2451 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE AMO A 831 |
| Chain | Residue |
| A | SER199 |
| A | GLN201 |
| A | LYS204 |
| A | ARG223 |
| A | GLU225 |
| A | ASP230 |
| A | ARG231 |
| A | GLN232 |
| A | PHE235 |
| A | GLN237 |
| A | HIS442 |
| A | HIS443 |
| A | GLU476 |
| A | GLY478 |
| A | GLY479 |
| A | GLY480 |
| A | ARG483 |
| A | ILE525 |
| A | ALA526 |
| A | GLY528 |
| A | ARG531 |
| A | HOH2027 |
| A | HOH2028 |
| A | HOH2224 |
| A | HOH2428 |
| A | GLU177 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE AMO B 1831 |
| Chain | Residue |
| B | GLU1177 |
| B | SER1199 |
| B | GLN1201 |
| B | LYS1204 |
| B | ARG1223 |
| B | GLU1225 |
| B | ASP1230 |
| B | ARG1231 |
| B | GLN1232 |
| B | PHE1235 |
| B | GLN1237 |
| B | HIS1442 |
| B | HIS1443 |
| B | GLU1476 |
| B | VAL1477 |
| B | GLY1478 |
| B | GLY1479 |
| B | GLY1480 |
| B | ARG1483 |
| B | ILE1525 |
| B | ALA1526 |
| B | GLY1528 |
| B | ARG1531 |
| B | HOH2013 |
| B | HOH2145 |
| B | HOH2265 |
| B | HOH2524 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AMP B 800 |
| Chain | Residue |
| B | PHE1311 |
| B | VAL1313 |
| B | GLU1338 |
| B | GLN1347 |
| B | GLY1348 |
| B | LEU1349 |
| B | ALA1350 |
| B | PHE1388 |
| B | VAL1389 |
| B | ALA1390 |
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 | GLN1232 | |
| B | HIS1442 | |
| B | GLU1476 | |
| B | ARG1483 | |
| B | GLY1528 | |
| A | ARG223 | |
| A | GLN232 | |
| A | HIS442 | |
| A | GLU476 | |
| A | ARG483 | |
| A | GLY528 | |
| B | GLU1177 | |
| B | ARG1223 |
