1F7U
CRYSTAL STRUCTURE OF THE ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNA(ARG) AND L-ARG
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 | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006420 | biological_process | arginyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0032543 | biological_process | mitochondrial translation |
| A | 1990825 | molecular_function | sequence-specific mRNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 900 |
| Chain | Residue |
| B | G907 |
| B | 5MC949 |
| B | HOH1314 |
| B | HOH1364 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ARG A 800 |
| Chain | Residue |
| A | ASP351 |
| A | TYR369 |
| A | ILE371 |
| A | GLN375 |
| A | HOH1321 |
| A | HOH1578 |
| B | A976 |
| A | GLU148 |
| A | SER151 |
| A | ASN153 |
| A | TYR188 |
| A | TYR347 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PniAKpFHAGHL |
| Chain | Residue | Details |
| A | PRO152-LEU163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Region: {"description":"Interaction with tRNA","evidences":[{"source":"PubMed","id":"11060012","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Motif: {"description":"'HIGH' region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11060012","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9736621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F7U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9736621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BS2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11060012, 9736621, 12554668, 16427818, 11106639 |
| Chain | Residue | Details |
| A | LYS156 | |
| A | HIS162 | |
| A | HIS159 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 235 |
| Chain | Residue | Details |
