Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004824 | molecular_function | lysine-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 | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0036260 | biological_process | RNA capping |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 515 |
| Chain | Residue |
| A | GLU414 |
| A | GLU421 |
| A | ATP512 |
| A | MN517 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 516 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 517 |
| Chain | Residue |
| A | GLU421 |
| A | ATP512 |
| A | MN515 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LYS A 510 |
| Chain | Residue |
| A | ALA217 |
| A | GLU240 |
| A | ARG262 |
| A | GLU278 |
| A | TYR280 |
| A | ASN424 |
| A | PHE426 |
| A | GLU428 |
| A | GLY473 |
| A | ATP512 |
| A | HOH2355 |
| A | GLY216 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 512 |
| Chain | Residue |
| A | ARG262 |
| A | GLU264 |
| A | ARG269 |
| A | HIS270 |
| A | ASN271 |
| A | PHE274 |
| A | MET276 |
| A | GLU421 |
| A | ILE422 |
| A | ASN424 |
| A | GLY477 |
| A | ARG480 |
| A | ILE491 |
| A | LYS510 |
| A | MN515 |
| A | MN516 |
| A | MN517 |
| A | HOH2198 |
| A | HOH2200 |
| A | HOH2356 |
| A | HOH2358 |
| A | HOH2359 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 520 |
| Chain | Residue |
| A | LEU190 |
| A | ARG194 |
| A | ARG194 |
| A | GLU204 |
| A | GLU206 |
| A | ILE257 |
| A | ASN258 |
| A | ASN258 |
| A | HOH2165 |
| A | HOH2196 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 521 |
| Chain | Residue |
| A | PRO214 |
| A | GLY215 |
| A | ALA217 |
| A | SER218 |
| A | ALA219 |
| A | ILE237 |
| A | LYS446 |
| A | GLU452 |
| A | ALA453 |
| A | MET454 |
| A | PHE455 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE415 | |
| A | ILE422 | |
| Chain | Residue | Details |
| A | LYS114 | |
| A | PHE156 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| A | ARG480 | |
| A | GLU278 | |
| A | ARG262 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| A | ARG262 | |
