4J15
Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0004046 | molecular_function | aminoacylase activity |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004815 | molecular_function | aspartate-tRNA ligase activity |
A | 0005515 | molecular_function | protein binding |
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 | 0016020 | cellular_component | membrane |
A | 0016874 | molecular_function | ligase activity |
A | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
A | 0045202 | cellular_component | synapse |
A | 0065003 | biological_process | protein-containing complex assembly |
A | 0070062 | cellular_component | extracellular exosome |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003723 | molecular_function | RNA binding |
B | 0004046 | molecular_function | aminoacylase activity |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004815 | molecular_function | aspartate-tRNA ligase activity |
B | 0005515 | molecular_function | protein binding |
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 | 0016020 | cellular_component | membrane |
B | 0016874 | molecular_function | ligase activity |
B | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
B | 0045202 | cellular_component | synapse |
B | 0065003 | biological_process | protein-containing complex assembly |
B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | ARG63 |
A | ALA64 |
A | GLN82 |
A | HOH783 |
A | HOH876 |
B | ASP261 |
B | GOL602 |
B | HOH819 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 602 |
Chain | Residue |
A | VAL144 |
A | ILE145 |
A | SER146 |
A | LEU147 |
B | ASP434 |
B | HOH852 |
A | SER32 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 603 |
Chain | Residue |
A | GLN199 |
A | GLU474 |
A | SER490 |
A | MET491 |
A | PHE492 |
B | GLN219 |
B | PRO221 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 604 |
Chain | Residue |
A | LYS40 |
A | GOL605 |
B | HIS300 |
B | ARG345 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 605 |
Chain | Residue |
A | GLN38 |
A | GOL604 |
A | HOH843 |
B | ARG408 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 601 |
Chain | Residue |
A | HIS204 |
A | ARG207 |
A | GLU208 |
A | ILE211 |
A | HOH768 |
B | HIS204 |
B | ARG207 |
B | HOH799 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 602 |
Chain | Residue |
A | ARG63 |
A | GLN82 |
A | GOL601 |
B | PHE295 |
B | ASN296 |
B | HOH841 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 603 |
Chain | Residue |
A | TYR297 |
B | ARG43 |
B | ASP115 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU229 | |
B | ARG281 | |
B | GLU424 | |
B | SER427 | |
B | ARG431 | |
B | GLY472 | |
A | ARG273 | |
A | ARG281 | |
A | GLU424 | |
A | SER427 | |
A | ARG431 | |
A | GLY472 | |
B | GLU229 | |
B | ARG273 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR52 | |
B | THR52 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS74 | |
A | LYS374 | |
B | LYS74 | |
B | LYS374 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER249 | |
B | SER249 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKA => ECO:0000255 |
Chain | Residue | Details |
A | THR500 | |
B | THR500 |