6NRZ
Crystal Structure of Lysyl-tRNA Synthetase from Chlamydia trachomatis complexed with L-lysine and Adenosine
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 | 0003877 | molecular_function | ATP:ADP adenylyltransferase activity |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004824 | molecular_function | lysine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005615 | cellular_component | extracellular space |
| 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 | 0015966 | biological_process | diadenosine tetraphosphate biosynthetic process |
| A | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| A | 0043032 | biological_process | positive regulation of macrophage activation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003877 | molecular_function | ATP:ADP adenylyltransferase activity |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004824 | molecular_function | lysine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005615 | cellular_component | extracellular space |
| 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 | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| B | 0015966 | biological_process | diadenosine tetraphosphate biosynthetic process |
| B | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| B | 0043032 | biological_process | positive regulation of macrophage activation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue LYS A 601 |
| Chain | Residue |
| A | GLY225 |
| A | GLY493 |
| A | ADN602 |
| A | GLU249 |
| A | ARG271 |
| A | GLU287 |
| A | TYR289 |
| A | ASN441 |
| A | TYR443 |
| A | GLU445 |
| A | GLY491 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue ADN A 602 |
| Chain | Residue |
| A | ARG271 |
| A | THR278 |
| A | HIS279 |
| A | ASN280 |
| A | PHE283 |
| A | MET285 |
| A | GLU438 |
| A | LEU439 |
| A | CYS440 |
| A | GLY495 |
| A | ARG498 |
| A | ILE509 |
| A | LYS601 |
| A | HOH821 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | PHE76 |
| A | ILE120 |
| A | GLU121 |
| A | LEU124 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | ILE183 |
| A | HOH948 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | ARG197 |
| A | LYS200 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | GLU213 |
| A | GLU215 |
| A | HOH776 |
| B | ARG203 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue PG4 A 607 |
| Chain | Residue |
| A | GLY225 |
| A | ALA226 |
| A | GLU227 |
| A | THR412 |
| A | THR413 |
| A | PRO414 |
| A | ARG429 |
| A | TYR443 |
| A | GLN459 |
| A | ASP475 |
| A | HOH798 |
| A | HOH806 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | PHE391 |
| A | ASP392 |
| A | GLU431 |
| A | HOH710 |
| A | HOH941 |
| A | HOH946 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 609 |
| Chain | Residue |
| A | TYR322 |
| A | LEU325 |
| A | LEU435 |
| A | LYS437 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 610 |
| Chain | Residue |
| A | LYS344 |
| A | ILE387 |
| A | THR425 |
| A | LEU426 |
| A | HOH708 |
| A | HOH784 |
| A | HOH786 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 611 |
| Chain | Residue |
| A | LEU450 |
| A | ARG453 |
| A | CYS483 |
| A | HOH877 |
| B | TYR7 |
| B | LEU8 |
| B | TYR13 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 612 |
| Chain | Residue |
| A | GLN220 |
| A | ALA251 |
| A | LYS254 |
| A | EDO613 |
| A | HOH701 |
| A | HOH905 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 613 |
| Chain | Residue |
| A | LEU219 |
| A | GLN220 |
| A | MET242 |
| A | EDO612 |
| A | HOH722 |
| A | HOH832 |
| B | PHE515 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 614 |
| Chain | Residue |
| A | LYS344 |
| A | ASP354 |
| A | VAL355 |
| A | ASP356 |
| A | HOH746 |
| A | HOH898 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 615 |
| Chain | Residue |
| A | LYS200 |
| A | GLU204 |
| A | HOH757 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 616 |
| Chain | Residue |
| B | LEU219 |
| B | GLN220 |
| B | MET242 |
| B | EDO1712 |
| A | PHE515 |
| A | PRO516 |
| A | HOH763 |
| A | HOH822 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 617 |
| Chain | Residue |
| A | GLU480 |
| B | ILE159 |
| B | HOH1857 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 618 |
| Chain | Residue |
| A | LYS463 |
| A | ASN466 |
| A | SER469 |
| A | HOH969 |
| A | HOH987 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 619 |
| Chain | Residue |
| A | GLU368 |
| A | THR371 |
| A | HOH719 |
| A | HOH972 |
| A | HOH1004 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1701 |
| Chain | Residue |
| A | ARG203 |
| B | GLU213 |
| B | GLU215 |
| B | HOH1924 |
| site_id | AE3 |
| Number of Residues | 10 |
| Details | binding site for residue LYS B 1702 |
| Chain | Residue |
| B | GLY225 |
| B | SER247 |
| B | GLU249 |
| B | ARG271 |
| B | GLU287 |
| B | TYR289 |
| B | ASN441 |
| B | TYR443 |
| B | GLU445 |
| B | ADN1703 |
| site_id | AE4 |
| Number of Residues | 14 |
| Details | binding site for residue ADN B 1703 |
| Chain | Residue |
| B | ARG271 |
| B | THR278 |
| B | HIS279 |
| B | ASN280 |
| B | PHE283 |
| B | MET285 |
| B | GLU438 |
| B | LEU439 |
| B | CYS440 |
| B | GLY495 |
| B | ARG498 |
| B | ILE509 |
| B | LYS1702 |
| B | HOH1919 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1704 |
| Chain | Residue |
| B | ASN304 |
| B | GLU307 |
| B | TYR308 |
| B | ARG311 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1705 |
| Chain | Residue |
| B | ASP392 |
| B | GLU431 |
| B | HOH1831 |
| B | HOH1837 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1706 |
| Chain | Residue |
| B | ARG24 |
| B | ASN29 |
| B | HOH1884 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 1707 |
| Chain | Residue |
| A | TYR7 |
| A | LEU8 |
| A | TYR13 |
| B | PRO449 |
| B | LEU450 |
| B | ARG453 |
| B | CYS483 |
| site_id | AE9 |
| Number of Residues | 10 |
| Details | binding site for residue PG4 B 1708 |
| Chain | Residue |
| B | TYR223 |
| B | GLY225 |
| B | ALA226 |
| B | THR412 |
| B | THR413 |
| B | PRO414 |
| B | LEU415 |
| B | TYR443 |
| B | GLN459 |
| B | ASP475 |
| site_id | AF1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 1709 |
| Chain | Residue |
| B | PHE76 |
| B | ILE120 |
| B | GLU121 |
| B | LEU124 |
| B | ASP125 |
| B | HOH1801 |
| B | HOH1907 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1710 |
| Chain | Residue |
| B | LYS164 |
| B | ILE183 |
| B | SER184 |
| B | HOH1804 |
| B | HOH1815 |
| site_id | AF3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1711 |
| Chain | Residue |
| A | HOH780 |
| B | PRO162 |
| B | ASP170 |
| B | ARG174 |
| B | HOH1891 |
| site_id | AF4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1712 |
| Chain | Residue |
| A | PHE515 |
| A | EDO616 |
| B | GLN220 |
| B | ALA251 |
| B | LYS254 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1713 |
| Chain | Residue |
| B | PRO32 |
| B | TYR33 |
| B | GLN34 |
| B | HOH1825 |
| site_id | AF6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1714 |
| Chain | Residue |
| B | ILE28 |
| B | ASN29 |
| B | HOH1847 |
| site_id | AF7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1715 |
| Chain | Residue |
| B | HIS10 |
| B | GLU11 |
| B | ASP12 |
| site_id | AF8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 1716 |
| Chain | Residue |
| B | LYS344 |
| B | ARG383 |
| B | THR425 |
| site_id | AF9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1717 |
| Chain | Residue |
| B | GLU303 |
| B | PRO337 |
| B | TRP338 |
| B | ARG340 |
| site_id | AG1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 1718 |
| Chain | Residue |
| B | LEU168 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00252 |
| Chain | Residue | Details |
| B | GLU431 | |
| B | GLU438 | |
| A | GLU431 | |
| A | GLU438 |
