Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000049 | molecular_function | tRNA binding |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004818 | molecular_function | glutamate-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 | 0006424 | biological_process | glutamyl-tRNA aminoacylation |
A | 0008270 | molecular_function | zinc ion binding |
A | 0043039 | biological_process | tRNA aminoacylation |
B | 0000049 | molecular_function | tRNA binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004818 | molecular_function | glutamate-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 | 0006424 | biological_process | glutamyl-tRNA aminoacylation |
B | 0008270 | molecular_function | zinc ion binding |
B | 0043039 | biological_process | tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 700 |
Chain | Residue |
C | HOH2317 |
C | HOH2318 |
C | HOH2319 |
C | HOH2320 |
C | HOH2321 |
C | HOH2322 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 701 |
Chain | Residue |
D | HOH2326 |
D | HOH2327 |
D | HOH2328 |
D | HOH2323 |
D | HOH2324 |
D | HOH2325 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE GOM A 600 |
Chain | Residue |
A | ARG5 |
A | ALA7 |
A | PRO8 |
A | SER9 |
A | GLY17 |
A | THR18 |
A | ILE21 |
A | GLU41 |
A | TYR187 |
A | ASN191 |
A | ARG205 |
A | ALA206 |
A | GLU208 |
A | TRP209 |
A | LEU235 |
A | LEU236 |
A | ILE244 |
A | HOH1122 |
A | HOH1294 |
A | HOH1360 |
A | HOH1480 |
C | A576 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GOM B 601 |
Chain | Residue |
B | ARG5 |
B | ALA7 |
B | SER9 |
B | GLY17 |
B | THR18 |
B | ILE21 |
B | GLU41 |
B | TYR187 |
B | ASN191 |
B | ARG205 |
B | ALA206 |
B | GLU208 |
B | TRP209 |
B | LEU235 |
B | LEU236 |
B | ILE244 |
B | HOH1137 |
B | HOH1256 |
B | HOH1624 |
D | A576 |
Functional Information from PROSITE/UniProt
site_id | PS00178 |
Number of Residues | 12 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGdPHVGTA |
Chain | Residue | Details |
A | PRO8-ALA19 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG5 | |
B | HIS15 | |
B | GLU41 | |
B | TYR187 | |
B | ARG205 | |
B | GLU208 | |
B | LEU236 | |
B | LYS243 | |
A | HIS15 | |
A | GLU41 | |
A | TYR187 | |
A | ARG205 | |
A | GLU208 | |
A | LEU236 | |
A | LYS243 | |
B | ARG5 | |
Chain | Residue | Details |
A | LYS246 | |
B | LYS246 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Interaction with tRNA; via carbonyl oxygen |
Chain | Residue | Details |
A | LEU354 | |
B | LEU354 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Essential for discrimination between tRNA(Glu) and tRNA(Gln) |
Chain | Residue | Details |
A | ARG358 | |
B | ARG358 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j09 |
Chain | Residue | Details |
A | LYS246 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j09 |
Chain | Residue | Details |
B | LYS246 | |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 318 |
Chain | Residue | Details |
A | LYS246 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 318 |
Chain | Residue | Details |
B | LYS246 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity |