1SZ1
Mechanism of CCA-adding enzymes specificity revealed by crystal structures of ternary complexes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001680 | biological_process | tRNA 3'-terminal CCA addition |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004810 | molecular_function | CCA tRNA nucleotidyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008033 | biological_process | tRNA processing |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0031123 | biological_process | RNA 3'-end processing |
| A | 0042245 | biological_process | RNA repair |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106354 | biological_process | tRNA surveillance |
| A | 0160016 | molecular_function | CCACCA tRNA nucleotidyltransferase activity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001680 | biological_process | tRNA 3'-terminal CCA addition |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004810 | molecular_function | CCA tRNA nucleotidyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008033 | biological_process | tRNA processing |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0031123 | biological_process | RNA 3'-end processing |
| B | 0042245 | biological_process | RNA repair |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0106354 | biological_process | tRNA surveillance |
| B | 0160016 | molecular_function | CCACCA tRNA nucleotidyltransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14592988, ECO:0000269|PubMed:14636575, ECO:0000269|PubMed:25640237, ECO:0007744|PDB:1R89, ECO:0007744|PDB:1UEU, ECO:0007744|PDB:4X4O, ECO:0007744|PDB:4X4Q, ECO:0007744|PDB:4X4S |
| Chain | Residue | Details |
| A | SER47 | |
| B | SER47 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14592988, ECO:0000269|PubMed:14636575, ECO:0000269|PubMed:25640237, ECO:0007744|PDB:1R89, ECO:0007744|PDB:1UEU, ECO:0007744|PDB:4X4Q, ECO:0007744|PDB:4X4S |
| Chain | Residue | Details |
| A | ARG50 | |
| A | HIS133 | |
| A | LYS152 | |
| A | TYR161 | |
| B | ARG50 | |
| B | HIS133 | |
| B | LYS152 | |
| B | TYR161 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14592988, ECO:0007744|PDB:1UEV |
| Chain | Residue | Details |
| A | GLU59 | |
| B | GLU59 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14592988, ECO:0007744|PDB:1R89, ECO:0007744|PDB:1UEV |
| Chain | Residue | Details |
| A | ASP61 | |
| A | ASP110 | |
| B | ASP61 | |
| B | ASP110 |
