6ILD
Crystal Structure of Human LysRS: P38/AIMP2 Complex II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide 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 | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004824 | molecular_function | lysine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| C | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue LYS A 601 |
| Chain | Residue |
| A | GLY277 |
| A | TRP547 |
| A | GOL605 |
| A | HOH939 |
| A | ALA278 |
| A | GLU301 |
| A | GLU339 |
| A | TYR341 |
| A | ASN497 |
| A | TYR499 |
| A | GLU501 |
| A | GLY546 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | HIS133 |
| A | GLY149 |
| A | GLU150 |
| A | GLY151 |
| A | ILE235 |
| A | ARG241 |
| A | HOH734 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | ARG323 |
| A | THR330 |
| A | HIS331 |
| A | ASN332 |
| A | PHE335 |
| A | HOH737 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 604 |
| Chain | Residue |
| A | GLU487 |
| A | GLU494 |
| A | HOH782 |
| A | HOH942 |
| A | HOH1020 |
| A | HOH1023 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | THR337 |
| A | GLU494 |
| A | ILE495 |
| A | CYS496 |
| A | ASN497 |
| A | GLY548 |
| A | GLY550 |
| A | LYS601 |
| A | HOH785 |
| A | HOH904 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue LYS B 601 |
| Chain | Residue |
| B | GLY277 |
| B | ALA278 |
| B | GLU301 |
| B | GLU339 |
| B | TYR341 |
| B | ASN497 |
| B | TYR499 |
| B | GLU501 |
| B | GLY546 |
| B | GOL603 |
| B | 45A605 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 602 |
| Chain | Residue |
| B | GLU487 |
| B | GLU494 |
| B | 45A605 |
| B | HOH740 |
| B | HOH763 |
| B | HOH962 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| B | THR337 |
| B | GLU494 |
| B | ILE495 |
| B | CYS496 |
| B | ASN497 |
| B | GLY548 |
| B | MET549 |
| B | GLY550 |
| B | LYS601 |
| B | 45A605 |
| B | HOH770 |
| B | HOH866 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 604 |
| Chain | Residue |
| B | TYR347 |
| B | ARG393 |
| B | ASN395 |
| B | ASP464 |
| B | HOH716 |
| B | HOH892 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue 45A B 605 |
| Chain | Residue |
| B | ARG323 |
| B | THR330 |
| B | HIS331 |
| B | ASN332 |
| B | PHE335 |
| B | GLU494 |
| B | ARG553 |
| B | ILE564 |
| B | LYS601 |
| B | MG602 |
| B | GOL603 |
| B | HOH763 |
| B | HOH771 |
| B | HOH831 |
| B | HOH960 |
| B | HOH962 |
| B | HOH981 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:26074468 |
| Chain | Residue | Details |
| A | GLY277 | |
| B | GLY277 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:26074468 |
| Chain | Residue | Details |
| A | GLU301 | |
| B | GLU501 | |
| A | GLU339 | |
| A | TYR341 | |
| A | ASN497 | |
| A | GLU501 | |
| B | GLU301 | |
| B | GLU339 | |
| B | TYR341 | |
| B | ASN497 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479 |
| Chain | Residue | Details |
| A | ARG323 | |
| A | HIS331 | |
| A | GLU494 | |
| A | GLY550 | |
| B | ARG323 | |
| B | HIS331 | |
| B | GLU494 | |
| B | GLY550 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS88 | |
| A | LYS141 | |
| B | LYS88 | |
| B | LYS141 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539 |
| Chain | Residue | Details |
| A | SER207 | |
| B | SER207 |
