6ILH
Crystal Structure of human lysyl-tRNA synthetase L350H 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 |
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 | THR337 |
A | GLU339 |
A | TYR341 |
A | GLU494 |
A | ILE495 |
A | ASN497 |
A | TYR499 |
A | GLU501 |
A | GLY546 |
A | GLY550 |
A | ALA299 |
A | ARG553 |
A | ILE564 |
A | HOH732 |
A | GLU301 |
A | ARG323 |
A | GLU325 |
A | THR330 |
A | HIS331 |
A | ASN332 |
A | PHE335 |
site_id | AC2 |
Number of Residues | 19 |
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 |
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 |