3OUY
How the CCA-adding Enzyme Selects Adenine Over Cytosine at Position 76 of tRNA
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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | ARG299 |
| A | ARG302 |
| A | LYS303 |
| A | HOH475 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | VAL289 |
| A | ASP290 |
| A | HOH456 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 801 |
| Chain | Residue |
| A | LEU65 |
| A | VAL40 |
| A | GLU41 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 603 |
| Chain | Residue |
| B | ARG299 |
| B | ARG302 |
| B | LYS303 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE POP B 702 |
| Chain | Residue |
| B | GLY46 |
| B | SER47 |
| B | ASP61 |
| B | LYS152 |
| B | TYR161 |
| D | A35 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE POP C 701 |
| Chain | Residue |
| A | GLY46 |
| A | SER47 |
| A | ASP61 |
| A | LYS152 |
| A | TYR161 |
| A | HOH543 |
| C | A35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 |
| B | SER47 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 |
| B | ARG50 | |
| B | HIS133 | |
| B | LYS152 | |
| B | TYR161 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14592988, ECO:0007744|PDB:1UEV |
| Chain | Residue | Details |
| B | GLU59 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14592988, ECO:0007744|PDB:1R89, ECO:0007744|PDB:1UEV |
| Chain | Residue | Details |
| B | ASP61 | |
| B | ASP110 |
