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 | 5 |
Details | BINDING SITE FOR RESIDUE MG A 515 |
Chain | Residue |
A | ARG412 |
A | GLU414 |
A | GLU421 |
A | ACP512 |
A | MG517 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 516 |
Chain | Residue |
A | GLU264 |
A | ACP512 |
A | HOH2172 |
A | HOH2303 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 517 |
Chain | Residue |
A | GLU421 |
A | ACP512 |
A | MG515 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LYS A 510 |
Chain | Residue |
A | GLY216 |
A | ALA217 |
A | GLU240 |
A | ARG262 |
A | MET276 |
A | GLU278 |
A | TYR280 |
A | ASN424 |
A | PHE426 |
A | GLU428 |
A | GLY473 |
A | ACP512 |
A | GOL523 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ACP A 512 |
Chain | Residue |
A | ARG262 |
A | GLU264 |
A | ARG269 |
A | HIS270 |
A | ASN271 |
A | PHE274 |
A | GLU380 |
A | GLU414 |
A | GLU421 |
A | ILE422 |
A | GLY477 |
A | ARG480 |
A | ILE491 |
A | LYS510 |
A | MG515 |
A | MG516 |
A | MG517 |
A | GOL523 |
A | HOH2258 |
A | HOH2302 |
A | HOH2303 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 520 |
Chain | Residue |
A | TYR312 |
A | HIS315 |
A | ILE384 |
A | GLY418 |
A | ARG420 |
A | HIS489 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 521 |
Chain | Residue |
A | ARG194 |
A | ARG194 |
A | GLU204 |
A | GLU206 |
A | ILE257 |
A | ASN258 |
A | ASN258 |
A | HOH2169 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 522 |
Chain | Residue |
A | TYR286 |
A | GLU391 |
A | ASN403 |
A | THR410 |
A | ASP411 |
A | ARG412 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 523 |
Chain | Residue |
A | ALA217 |
A | SER218 |
A | VAL396 |
A | ARG412 |
A | ASN424 |
A | PHE426 |
A | LYS510 |
A | ACP512 |
A | HOH2152 |
A | HOH2305 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GOL A 524 |
Chain | Residue |
A | PRO214 |
A | GLY215 |
A | ALA217 |
A | SER218 |
A | ALA219 |
A | PRO221 |
A | ILE237 |
A | LYS446 |
A | GLU452 |
A | ALA453 |
A | MET454 |
A | PHE455 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 525 |
Chain | Residue |
A | VAL33 |
A | LYS333 |
A | ARG402 |
A | ASN403 |
A | ASP404 |
A | HOH2250 |
A | HOH2306 |
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 | |