7EA9
Crystal Structure of human lysyl-tRNA synthetase Y145H mutant
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 | 22 |
Details | binding site for residue KAA A 601 |
Chain | Residue |
A | GLY277 |
A | GLU339 |
A | TYR341 |
A | GLU494 |
A | ILE495 |
A | ASN497 |
A | TYR499 |
A | GLU501 |
A | GLY546 |
A | GLY550 |
A | ARG553 |
A | GLU301 |
A | ILE564 |
A | GOL602 |
A | HOH796 |
A | ARG323 |
A | GLU325 |
A | THR330 |
A | HIS331 |
A | ASN332 |
A | PHE335 |
A | THR337 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue GOL A 602 |
Chain | Residue |
A | HIS331 |
A | GLU494 |
A | ARG553 |
A | KAA601 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue KAA B 601 |
Chain | Residue |
B | GLY277 |
B | GLU301 |
B | ARG323 |
B | GLU325 |
B | THR330 |
B | HIS331 |
B | ASN332 |
B | PHE335 |
B | THR337 |
B | GLU339 |
B | TYR341 |
B | GLU494 |
B | ILE495 |
B | ASN497 |
B | TYR499 |
B | GLU501 |
B | GLY546 |
B | GLY550 |
B | ARG553 |
B | ILE564 |
B | GOL602 |
B | HOH774 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 602 |
Chain | Residue |
B | ARG323 |
B | GLU325 |
B | HIS331 |
B | ARG553 |
B | KAA601 |
site_id | AC5 |
Number of Residues | 22 |
Details | binding site for residue KAA C 601 |
Chain | Residue |
C | GLY277 |
C | GLU301 |
C | ARG323 |
C | GLU325 |
C | THR330 |
C | HIS331 |
C | ASN332 |
C | PHE335 |
C | THR337 |
C | GLU339 |
C | TYR341 |
C | GLU494 |
C | ILE495 |
C | ASN497 |
C | TYR499 |
C | GLU501 |
C | GLY546 |
C | GLY550 |
C | ARG553 |
C | ILE564 |
C | GOL602 |
C | HOH763 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL C 602 |
Chain | Residue |
C | ARG323 |
C | GLU325 |
C | HIS331 |
C | GLU494 |
C | KAA601 |
site_id | AC7 |
Number of Residues | 23 |
Details | binding site for residue KAA D 601 |
Chain | Residue |
D | ARG553 |
D | ILE564 |
D | GOL602 |
D | HOH788 |
D | GLY277 |
D | GLU301 |
D | ARG323 |
D | GLU325 |
D | THR330 |
D | HIS331 |
D | ASN332 |
D | PHE335 |
D | THR337 |
D | GLU339 |
D | TYR341 |
D | GLU494 |
D | ILE495 |
D | ASN497 |
D | TYR499 |
D | GLU501 |
D | GLY546 |
D | GLY548 |
D | GLY550 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue GOL D 602 |
Chain | Residue |
D | GLU325 |
D | HIS331 |
D | ARG553 |
D | KAA601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:26074468 |
Chain | Residue | Details |
A | GLY277 | |
B | GLY277 | |
C | GLY277 | |
D | GLY277 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:26074468 |
Chain | Residue | Details |
A | GLU301 | |
B | GLU501 | |
C | GLU301 | |
C | GLU339 | |
C | TYR341 | |
C | ASN497 | |
C | GLU501 | |
D | GLU301 | |
D | GLU339 | |
D | TYR341 | |
D | ASN497 | |
A | GLU339 | |
D | GLU501 | |
A | TYR341 | |
A | ASN497 | |
A | GLU501 | |
B | GLU301 | |
B | GLU339 | |
B | TYR341 | |
B | ASN497 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18272479 |
Chain | Residue | Details |
A | ARG323 | |
C | HIS331 | |
C | GLU494 | |
C | GLY550 | |
D | ARG323 | |
D | HIS331 | |
D | GLU494 | |
D | GLY550 | |
A | HIS331 | |
A | GLU494 | |
A | GLY550 | |
B | ARG323 | |
B | HIS331 | |
B | GLU494 | |
B | GLY550 | |
C | ARG323 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS88 | |
A | LYS141 | |
B | LYS88 | |
B | LYS141 | |
C | LYS88 | |
C | LYS141 | |
D | LYS88 | |
D | LYS141 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539 |
Chain | Residue | Details |
A | SER207 | |
B | SER207 | |
C | SER207 | |
D | SER207 |