Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002055 | molecular_function | adenine binding |
| A | 0003999 | molecular_function | adenine phosphoribosyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0006168 | biological_process | adenine salvage |
| A | 0016208 | molecular_function | AMP binding |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0044209 | biological_process | AMP salvage |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0002055 | molecular_function | adenine binding |
| B | 0003999 | molecular_function | adenine phosphoribosyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006166 | biological_process | purine ribonucleoside salvage |
| B | 0006168 | biological_process | adenine salvage |
| B | 0016208 | molecular_function | AMP binding |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0044209 | biological_process | AMP salvage |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue IR9 A 201 |
| Chain | Residue |
| A | ARG69 |
| A | HOH306 |
| A | HOH310 |
| A | HOH328 |
| A | HOH329 |
| A | HOH331 |
| A | HOH335 |
| A | HOH353 |
| A | HOH355 |
| B | GLU106 |
| B | TYR107 |
| A | ASP129 |
| A | ASP130 |
| A | ILE131 |
| A | ALA133 |
| A | THR134 |
| A | GLY135 |
| A | GLY136 |
| A | SER137 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 202 |
| Chain | Residue |
| A | GLU52 |
| A | PHE55 |
| A | VAL58 |
| A | ILE60 |
| A | EDO203 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 203 |
| Chain | Residue |
| A | LYS59 |
| A | ILE60 |
| A | LEU81 |
| A | EDO202 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue IR9 B 201 |
| Chain | Residue |
| A | SER22 |
| B | ARG69 |
| B | ASP129 |
| B | ASP130 |
| B | ILE131 |
| B | ALA133 |
| B | THR134 |
| B | GLY135 |
| B | GLY136 |
| B | SER137 |
| B | HOH313 |
| B | HOH318 |
| B | HOH319 |
| B | HOH321 |
| B | HOH337 |
| B | HOH354 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 202 |
| Chain | Residue |
| B | PHE55 |
| B | PRO56 |
| B | VAL58 |
| B | ILE60 |
| B | EDO203 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 203 |
| Chain | Residue |
| B | VAL58 |
| B | LYS59 |
| B | ILE60 |
| B | LEU81 |
| B | VAL83 |
| B | EDO202 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 204 |
| Chain | Residue |
| B | PHE55 |
| B | GLU154 |
| B | PRO173 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 205 |
| Chain | Residue |
| A | GLN115 |
| A | ALA118 |
| B | LEU31 |
| B | ARG35 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 206 |
| Chain | Residue |
| A | PRO32 |
| A | ARG35 |
| B | GLN115 |
| B | ALA118 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue ADE B 207 |
| Chain | Residue |
| B | LEU26 |
| B | PHE27 |
| B | GLU28 |
| B | ARG69 |
| B | ILE131 |
| B | ALA133 |
| B | LEU161 |
| B | HOH333 |
| B | HOH365 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VIIVDDIIATGgS |
| Chain | Residue | Details |
| A | VAL125-SER137 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | ALA133 | |
| B | ALA133 | |
| Chain | Residue | Details |
| A | SER68 | |
| B | SER68 | |
