6WUF
Crystal structure of mouse DXO in complex with 3'-FADP
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 | 27 |
| Details | binding site for residue UBG A 401 |
| Chain | Residue |
| A | ARG95 |
| A | GLY233 |
| A | GLN234 |
| A | LYS255 |
| A | GLN280 |
| A | HOH505 |
| A | HOH515 |
| A | HOH530 |
| A | HOH535 |
| A | HOH562 |
| A | HOH568 |
| A | GLU97 |
| A | HOH570 |
| A | HOH582 |
| A | HOH588 |
| A | HOH596 |
| A | HOH633 |
| A | HOH655 |
| A | HOH669 |
| A | HOH725 |
| A | TRP131 |
| A | ARG132 |
| A | GLY133 |
| A | HIS134 |
| A | GLU166 |
| A | ARG174 |
| A | TYR189 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | TYR70 |
| A | HIS288 |
| A | THR305 |
| A | HOH545 |
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 | GLN234 | |
| 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 | SER192 | |
| 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 | GLN253 | |
| A | LEU254 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6MG77 |
| Chain | Residue | Details |
| A | THR392 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER394 |
