4J7L
Crystal structure of mouse DXO in complex with PRODUCT RNA AND two MAGNESIUM ions
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
A | 0003723 | molecular_function | RNA binding |
A | 0003729 | molecular_function | mRNA binding |
A | 0004527 | molecular_function | exonuclease activity |
A | 0005634 | cellular_component | nucleus |
A | 0005829 | cellular_component | cytosol |
A | 0006402 | biological_process | mRNA catabolic process |
A | 0008409 | molecular_function | 5'-3' exonuclease activity |
A | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050779 | biological_process | RNA destabilization |
A | 0071028 | biological_process | nuclear mRNA surveillance |
A | 0090304 | biological_process | nucleic acid metabolic process |
A | 0110152 | molecular_function | RNA NAD+-cap (NAD+-forming) hydrolase activity |
A | 0110155 | biological_process | NAD-cap decapping |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE UBD A 401 |
Chain | Residue |
A | ARG30 |
A | THR31 |
A | GLN32 |
A | GLY358 |
A | GLY359 |
A | PRO360 |
A | HOH662 |
A | HOH819 |
A | HOH823 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | ASP236 |
A | GLU253 |
A | LEU254 |
A | HOH501 |
B | U2 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 403 |
Chain | Residue |
A | GLU234 |
A | ASP236 |
A | HOH503 |
A | HOH504 |
B | U2 |
B | HOH101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:28283058 |
Chain | Residue | Details |
A | ARG58 | |
A | TRP131 | |
A | GLU234 | |
A | LYS255 | |
A | GLN280 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23523372 |
Chain | Residue | Details |
A | GLU101 | |
A | GLU192 | |
A | CYS217 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30180947 |
Chain | Residue | Details |
A | MET185 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947 |
Chain | Residue | Details |
A | ASP236 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947, ECO:0000305|PubMed:28283058 |
Chain | Residue | Details |
A | GLU253 | |
A | LEU254 |