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 | TRP131 | |
A | GLN234 | |
A | LYS255 | |
A | GLN280 | |
A | ARG58 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23523372 |
Chain | Residue | Details |
A | CYS217 | |
A | SER192 | |
A | GLU101 |
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 | LEU254 | |
A | GLN253 |
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 |