Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004651 | molecular_function | polynucleotide 5'-phosphatase activity |
| B | 0004651 | molecular_function | polynucleotide 5'-phosphatase activity |
| C | 0004651 | molecular_function | polynucleotide 5'-phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | ARG393 |
| A | LYS409 |
| A | LYS456 |
| A | ARG458 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 602 |
| Chain | Residue |
| B | ARG393 |
| B | LYS409 |
| B | LYS456 |
| B | ARG458 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 603 |
| Chain | Residue |
| C | GLN405 |
| C | LYS409 |
| C | LYS456 |
| C | ARG458 |
| C | HOH697 |
| C | HOH698 |
| C | ARG393 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | GLN249 |
| A | LYS250 |
| A | TRP251 |
| A | TYR294 |
| A | HOH607 |
| A | HOH642 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 605 |
| Chain | Residue |
| A | TYR539 |
| B | GLN249 |
| B | LYS250 |
| B | TRP251 |
| B | TYR294 |
| B | HOH620 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 606 |
| Chain | Residue |
| C | GLN249 |
| C | LYS250 |
| C | TRP251 |
| C | TYR294 |
| C | HOH669 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | SITE: Essential for dimer formation |
| Chain | Residue | Details |
| A | ASP280 | |
| B | ASP280 | |
| C | ASP280 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d8h |
| Chain | Residue | Details |
| A | LYS456 | |
| A | GLU433 | |
| A | ARG458 | |
| A | ARG393 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d8h |
| Chain | Residue | Details |
| B | LYS456 | |
| B | GLU433 | |
| B | ARG458 | |
| B | ARG393 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d8h |
| Chain | Residue | Details |
| C | LYS456 | |
| C | GLU433 | |
| C | ARG458 | |
| C | ARG393 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 486 |
| Chain | Residue | Details |
| A | GLU305 | metal ligand |
| A | GLU307 | metal ligand |
| A | ARG393 | electrostatic stabiliser |
| A | LYS409 | electrostatic stabiliser |
| A | LYS456 | electrostatic stabiliser |
| A | GLU496 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 486 |
| Chain | Residue | Details |
| B | GLU305 | metal ligand |
| B | GLU307 | metal ligand |
| B | ARG393 | electrostatic stabiliser |
| B | LYS409 | electrostatic stabiliser |
| B | LYS456 | electrostatic stabiliser |
| B | GLU496 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 486 |
| Chain | Residue | Details |
| C | GLU305 | metal ligand |
| C | GLU307 | metal ligand |
| C | ARG393 | electrostatic stabiliser |
| C | LYS409 | electrostatic stabiliser |
| C | LYS456 | electrostatic stabiliser |
| C | GLU496 | metal ligand |
