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 | 1901576 | biological_process | organic substance biosynthetic process |
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 | 1901576 | biological_process | organic substance biosynthetic process |
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 | 14 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00044 |
Chain | Residue | Details |
A | GLU171 | |
B | GLN1226 | |
B | HIS1448 | |
B | GLU1482 | |
B | ARG1489 | |
B | GLY1534 | |
A | ARG217 | |
A | GLN226 | |
A | HIS448 | |
A | GLU482 | |
A | ARG489 | |
A | GLY534 | |
B | GLU1171 | |
B | ARG1217 |