5UJI
Crystal structure of human T2-Tryptophanyl-tRNA synthetase with H130R mutation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
Functional Information from PROSITE/UniProt
site_id | PS00178 |
Number of Residues | 11 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SEaMHVGHL |
Chain | Residue | Details |
A | PRO164-LEU174 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P32921 |
Chain | Residue | Details |
A | MET195 | |
B | MET195 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | GLY392 | |
B | GLY392 |