Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006397 | biological_process | mRNA processing |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0110155 | biological_process | NAD-cap decapping |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004527 | molecular_function | exonuclease activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006397 | biological_process | mRNA processing |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0110155 | biological_process | NAD-cap decapping |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 401 |
| Chain | Residue |
| B | ASP217 |
| B | GLU235 |
| B | LEU236 |
| B | HOH535 |
| D | U2 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 402 |
| Chain | Residue |
| B | HOH572 |
| D | U2 |
| B | GLU215 |
| B | ASP217 |
| B | HOH530 |
| B | HOH552 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 403 |
| Chain | Residue |
| B | HOH515 |
| B | HOH531 |
| B | HOH538 |
| B | HOH541 |
| B | HOH543 |
| B | HOH623 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 404 |
| Chain | Residue |
| B | ARG106 |
| B | GLY107 |
| B | LYS198 |
| B | GLY213 |
| B | ALA214 |
| B | GLU215 |
| B | HOH532 |
| B | HOH593 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MN C 401 |
| Chain | Residue |
| A | ASP217 |
| A | GLU235 |
| A | LEU236 |
| A | HOH540 |
| C | U2 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 402 |
| Chain | Residue |
| A | GLU215 |
| A | ASP217 |
| A | HOH527 |
| A | HOH536 |
| A | HOH598 |
| C | U2 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 401 |
| Chain | Residue |
| A | HOH504 |
| A | HOH522 |
| A | HOH539 |
| A | HOH545 |
| A | HOH565 |
| A | HOH604 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | ARG106 |
| A | GLY107 |
| A | LYS198 |
| A | GLY213 |
| A | ALA214 |
| A | GLU215 |
| A | HOH524 |
| A | HOH607 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O70348","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A3LNL5","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26101253","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BTE","evidenceCode":"ECO:0007744"}]} |
