1IL2
Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex
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 | 0005829 | cellular_component | cytosol |
| 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 |
| A | 0140640 | molecular_function | catalytic activity, acting on a nucleic acid |
| 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 | 0005829 | cellular_component | cytosol |
| 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 |
| B | 0140640 | molecular_function | catalytic activity, acting on a nucleic acid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 701 |
| Chain | Residue |
| A | ARG225 |
| A | GLU482 |
| A | ARG537 |
| A | AMO831 |
| C | C975 |
| C | A976 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1701 |
| Chain | Residue |
| B | ARG1537 |
| B | HOH2093 |
| B | HOH2097 |
| B | ARG1222 |
| B | ARG1225 |
| B | GLU1482 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE AMO A 831 |
| Chain | Residue |
| A | GLU171 |
| A | SER193 |
| A | GLN195 |
| A | LYS198 |
| A | ARG217 |
| A | ASP224 |
| A | ARG225 |
| A | GLN226 |
| A | PHE229 |
| A | GLN231 |
| A | HIS448 |
| A | HIS449 |
| A | GLU482 |
| A | VAL483 |
| A | GLY484 |
| A | GLY485 |
| A | ARG489 |
| A | GLY530 |
| A | LEU531 |
| A | ALA532 |
| A | GLY534 |
| A | ARG537 |
| A | HOH2328 |
| A | HOH2339 |
| C | SO4701 |
| C | A976 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE AMO B 1831 |
| Chain | Residue |
| B | GLU1171 |
| B | SER1193 |
| B | GLN1195 |
| B | LYS1198 |
| B | ARG1217 |
| B | GLU1219 |
| B | ASP1224 |
| B | ARG1225 |
| B | GLN1226 |
| B | PHE1229 |
| B | GLN1231 |
| B | HIS1448 |
| B | HIS1449 |
| B | GLU1482 |
| B | VAL1483 |
| B | GLY1484 |
| B | GLY1485 |
| B | GLY1486 |
| B | ARG1489 |
| B | GLY1530 |
| B | LEU1531 |
| B | ALA1532 |
| B | GLY1534 |
| B | ARG1537 |
| B | HOH2009 |
| B | HOH2015 |
| B | HOH2097 |
| B | HOH2398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Region: {"description":"Aspartate","evidences":[{"source":"HAMAP-Rule","id":"MF_00044","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00044","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| A | ARG217 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| B | ARG1217 |
