Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004829 | molecular_function | threonine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006435 | biological_process | threonyl-tRNA aminoacylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004829 | molecular_function | threonine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006435 | biological_process | threonyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | CYS334 |
A | HIS385 |
A | HIS511 |
A | HOH842 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 2 |
Chain | Residue |
B | CYS334 |
B | HIS385 |
B | HIS511 |
B | THR801 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE THR B 801 |
Chain | Residue |
B | MET332 |
B | CYS334 |
B | ARG363 |
B | GLN381 |
B | ASP383 |
B | HIS385 |
B | TYR462 |
B | THR482 |
B | GLN484 |
B | HIS511 |
B | HOH814 |
B | ZN2 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS246 | |
A | ASN342 | |
A | LEU489 | |
A | ASP615 | |
B | LYS246 | |
B | ASN342 | |
B | LEU489 | |
B | ASP615 | |
Chain | Residue | Details |
A | HIS309 | |
B | SER517 | |
A | VAL376 | |
A | GLN381 | |
A | GLN479 | |
A | SER517 | |
B | HIS309 | |
B | VAL376 | |
B | GLN381 | |
B | GLN479 | |
Chain | Residue | Details |
A | TYR313 | |
A | ILE547 | |
A | ASN575 | |
A | ARG589 | |
A | VAL595 | |
A | ARG609 | |
B | TYR313 | |
B | ARG325 | |
B | TYR348 | |
B | ARG363 | |
B | ARG375 | |
A | ARG325 | |
B | PHE379 | |
B | TYR462 | |
B | GLN484 | |
B | ARG520 | |
B | ILE547 | |
B | ASN575 | |
B | ARG589 | |
B | VAL595 | |
B | ARG609 | |
A | TYR348 | |
A | ARG363 | |
A | ARG375 | |
A | PHE379 | |
A | TYR462 | |
A | GLN484 | |
A | ARG520 | |
Chain | Residue | Details |
A | CYS334 | |
A | HIS385 | |
B | CYS334 | |
B | HIS385 | |
Chain | Residue | Details |
A | HIS511 | |
B | HIS511 | |
Chain | Residue | Details |
A | LYS286 | |
B | LYS286 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
A | ARG363 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
B | ARG363 | |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 540 |
Chain | Residue | Details |
A | CYS334 | electrostatic stabiliser, metal ligand |
A | ARG363 | electrostatic stabiliser |
A | GLN381 | electrostatic stabiliser |
A | ASP383 | electrostatic stabiliser |
A | HIS385 | metal ligand |
A | LYS465 | electrostatic stabiliser |
A | HIS511 | metal ligand |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 540 |
Chain | Residue | Details |
B | CYS334 | electrostatic stabiliser, metal ligand |
B | ARG363 | electrostatic stabiliser |
B | GLN381 | electrostatic stabiliser |
B | ASP383 | electrostatic stabiliser |
B | HIS385 | metal ligand |
B | LYS465 | electrostatic stabiliser |
B | HIS511 | metal ligand |