4Q2Y
Crystal structure of Arginyl-tRNA synthetase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004814 | molecular_function | arginine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006420 | biological_process | arginyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004814 | molecular_function | arginine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006420 | biological_process | arginyl-tRNA aminoacylation |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PniAKeMHVGHL |
| Chain | Residue | Details |
| A | PRO129-LEU140 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24859084, ECO:0007744|PDB:4Q2T |
| Chain | Residue | Details |
| A | PHE200 | |
| B | LYS412 | |
| A | GLU211 | |
| A | SER384 | |
| A | VAL388 | |
| A | LYS412 | |
| B | PHE200 | |
| B | GLU211 | |
| B | SER384 | |
| B | VAL388 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
