Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000290 | biological_process | deadenylation-dependent decapping of nuclear-transcribed mRNA |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0000290 | biological_process | deadenylation-dependent decapping of nuclear-transcribed mRNA |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue AJQ A 400 |
| Chain | Residue |
| A | ARG54 |
| A | ASP205 |
| A | LEU206 |
| A | LYS207 |
| A | TYR217 |
| A | ILE219 |
| A | HIS268 |
| A | SER272 |
| A | TYR273 |
| A | HIS277 |
| A | PRO288 |
| A | ASP59 |
| A | ARG294 |
| A | HOH513 |
| A | HOH611 |
| A | HOH612 |
| A | HOH615 |
| A | HOH629 |
| B | ARG58 |
| B | TYR113 |
| A | GLU85 |
| A | LYS142 |
| A | TYR143 |
| A | TRP175 |
| A | GLU185 |
| A | ARG188 |
| A | PRO204 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue AJQ B 401 |
| Chain | Residue |
| B | TRP175 |
| B | GLU185 |
| B | LEU206 |
| B | HOH556 |
| B | HOH571 |
| B | HOH603 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| A | LEU150 |
| A | ARG152 |
| B | LEU263 |
| B | VAL265 |
| B | LEU297 |
| B | LEU298 |
| B | ALA299 |
| B | GOL406 |
| B | HOH504 |
| B | HOH559 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| A | VAL190 |
| A | PHE191 |
| A | ALA251 |
| A | ARG255 |
| B | HOH564 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| A | LYS183 |
| A | GLN254 |
| B | LYS51 |
| B | GLU137 |
| B | LEU140 |
| B | GLN141 |
| B | LEU144 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| A | SER290 |
| A | GLY291 |
| B | GLU286 |
| B | SER290 |
| B | HOH503 |
| B | HOH534 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| A | LEU150 |
| B | GLN249 |
| B | GLY260 |
| B | ASP261 |
| B | GOL402 |
| B | HOH555 |
Functional Information from PROSITE/UniProt
| site_id | PS00892 |
| Number of Residues | 19 |
| Details | HIT_1 HIT domain signature. RvylhYlPsYyHLHVHFTA |
| Chain | Residue | Details |
| A | ARG264-ALA282 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | HIS277 | |
| B | HIS277 | |
| Chain | Residue | Details |
| A | TRP175 | |
| A | GLU185 | |
| A | ASP205 | |
| A | LYS207 | |
| B | TRP175 | |
| B | GLU185 | |
| B | ASP205 | |
| B | LYS207 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS268 | |
| B | HIS268 | |
| Chain | Residue | Details |
| A | SER101 | |
| B | SER101 | |
| Chain | Residue | Details |
| A | LYS138 | |
| A | LYS142 | |
| B | LYS138 | |
| B | LYS142 | |
