3BJU
Crystal Structure of tetrameric form of human lysyl-tRNA synthetase
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 | 0000166 | molecular_function | nucleotide binding |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004824 | molecular_function | lysine-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004824 | molecular_function | lysine-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006430 | biological_process | lysyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 606 |
| Chain | Residue |
| A | GLU487 |
| A | GLU494 |
| A | ATP603 |
| A | CA608 |
| A | HOH786 |
| A | HOH794 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 607 |
| Chain | Residue |
| A | ATP603 |
| A | HOH653 |
| A | HOH714 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 608 |
| Chain | Residue |
| A | GLU494 |
| A | ATP603 |
| A | CA606 |
| A | HOH674 |
| A | HOH786 |
| A | HOH824 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 606 |
| Chain | Residue |
| B | GLU487 |
| B | GLU494 |
| B | ATP603 |
| B | CA608 |
| B | HOH812 |
| B | HOH866 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 607 |
| Chain | Residue |
| B | ATP603 |
| B | HOH827 |
| B | HOH903 |
| B | HOH914 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 608 |
| Chain | Residue |
| B | GLU494 |
| B | ATP603 |
| B | CA606 |
| B | HOH812 |
| B | HOH840 |
| B | HOH843 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 606 |
| Chain | Residue |
| C | GLU487 |
| C | GLU494 |
| C | ATP603 |
| C | CA608 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 607 |
| Chain | Residue |
| C | ATP603 |
| C | HOH704 |
| C | HOH856 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 608 |
| Chain | Residue |
| C | GLU494 |
| C | ATP603 |
| C | CA606 |
| C | HOH670 |
| C | HOH838 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA D 607 |
| Chain | Residue |
| D | ATP603 |
| D | HOH752 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 606 |
| Chain | Residue |
| D | GLU487 |
| D | GLU494 |
| D | ATP603 |
| D | CA608 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 608 |
| Chain | Residue |
| D | GLU494 |
| D | ATP603 |
| D | CA606 |
| D | HOH699 |
| D | HOH759 |
| D | HOH770 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LYS A 601 |
| Chain | Residue |
| A | GLY277 |
| A | ALA278 |
| A | ALA299 |
| A | GLU301 |
| A | ARG323 |
| A | GLU339 |
| A | TYR341 |
| A | ASN497 |
| A | TYR499 |
| A | GLU501 |
| A | GLY546 |
| A | ATP603 |
| A | HOH698 |
| site_id | BC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP A 603 |
| Chain | Residue |
| A | ARG323 |
| A | GLU325 |
| A | THR330 |
| A | HIS331 |
| A | ASN332 |
| A | PHE335 |
| A | GLU494 |
| A | ILE495 |
| A | ASN497 |
| A | GLY550 |
| A | ARG553 |
| A | ILE564 |
| A | LYS601 |
| A | CA606 |
| A | CA607 |
| A | CA608 |
| A | HOH609 |
| A | HOH653 |
| A | HOH674 |
| A | HOH776 |
| A | HOH786 |
| A | HOH824 |
| A | HOH825 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LYS B 601 |
| Chain | Residue |
| B | TYR499 |
| B | GLU501 |
| B | GLY546 |
| B | ATP603 |
| B | HOH790 |
| B | GLY277 |
| B | ALA278 |
| B | ALA299 |
| B | GLU301 |
| B | ARG323 |
| B | GLU339 |
| B | TYR341 |
| B | ASN497 |
| site_id | BC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP B 603 |
| Chain | Residue |
| B | ARG323 |
| B | GLU325 |
| B | THR330 |
| B | HIS331 |
| B | ASN332 |
| B | PHE335 |
| B | GLU494 |
| B | ILE495 |
| B | ASN497 |
| B | GLY550 |
| B | ARG553 |
| B | LYS601 |
| B | CA606 |
| B | CA607 |
| B | CA608 |
| B | HOH678 |
| B | HOH740 |
| B | HOH812 |
| B | HOH827 |
| B | HOH843 |
| B | HOH875 |
| B | HOH914 |
| site_id | BC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LYS C 601 |
| Chain | Residue |
| C | GLY277 |
| C | ALA278 |
| C | ALA299 |
| C | GLU301 |
| C | ARG323 |
| C | GLU339 |
| C | TYR341 |
| C | ASN497 |
| C | TYR499 |
| C | GLU501 |
| C | GLY546 |
| C | ATP603 |
| C | HOH714 |
| site_id | BC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP C 603 |
| Chain | Residue |
| C | ARG323 |
| C | GLU325 |
| C | THR330 |
| C | HIS331 |
| C | ASN332 |
| C | PHE335 |
| C | GLU494 |
| C | ILE495 |
| C | ASN497 |
| C | GLY550 |
| C | ARG553 |
| C | ILE564 |
| C | LYS601 |
| C | CA606 |
| C | CA607 |
| C | CA608 |
| C | HOH609 |
| C | HOH670 |
| C | HOH678 |
| C | HOH797 |
| C | HOH856 |
| site_id | CC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LYS D 601 |
| Chain | Residue |
| D | GLY277 |
| D | ALA278 |
| D | ALA299 |
| D | GLU301 |
| D | GLU339 |
| D | TYR341 |
| D | ASN497 |
| D | TYR499 |
| D | GLU501 |
| D | GLY546 |
| D | GLY548 |
| D | ATP603 |
| D | HOH689 |
| site_id | CC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP D 603 |
| Chain | Residue |
| D | ARG323 |
| D | GLU325 |
| D | THR330 |
| D | HIS331 |
| D | ASN332 |
| D | PHE335 |
| D | GLU494 |
| D | ILE495 |
| D | ASN497 |
| D | GLY550 |
| D | ARG553 |
| D | LYS601 |
| D | CA606 |
| D | CA607 |
| D | CA608 |
| D | HOH610 |
| D | HOH687 |
| D | HOH699 |
| D | HOH752 |
| D | HOH759 |
| D | HOH797 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26074468","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23159739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26074468","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19524539","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| A | ARG323 | |
| A | ARG553 | |
| A | GLU339 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| B | ARG323 | |
| B | ARG553 | |
| B | GLU339 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| C | ARG323 | |
| C | ARG553 | |
| C | GLU339 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| D | ARG323 | |
| D | ARG553 | |
| D | GLU339 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| A | ARG323 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| B | ARG323 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| C | ARG323 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| D | ARG323 |
