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 | 9 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P32921","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
