Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004766 | molecular_function | spermidine synthase activity |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004766 | molecular_function | spermidine synthase activity |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004766 | molecular_function | spermidine synthase activity |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004766 | molecular_function | spermidine synthase activity |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue S4M A 501 |
| Chain | Residue |
| A | GLN40 |
| A | VAL123 |
| A | ASP149 |
| A | GLY150 |
| A | ASP168 |
| A | THR169 |
| A | THR170 |
| A | PRO175 |
| A | ALA176 |
| A | LEU179 |
| A | TYR237 |
| A | LEU59 |
| A | BSX502 |
| A | GLN64 |
| A | HIS74 |
| A | GLY95 |
| A | ASP98 |
| A | ASP118 |
| A | ILE119 |
| A | ASP120 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue BSX A 502 |
| Chain | Residue |
| A | TRP19 |
| A | GLN64 |
| A | TYR73 |
| A | THR169 |
| A | THR170 |
| A | ASP171 |
| A | GLN201 |
| A | TYR237 |
| A | PRO238 |
| A | S4M501 |
| A | HOH618 |
| A | HOH626 |
| A | HOH689 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue S4M B 501 |
| Chain | Residue |
| B | GLN40 |
| B | MET57 |
| B | LEU59 |
| B | GLN64 |
| B | TYR73 |
| B | HIS74 |
| B | GLY95 |
| B | ASP98 |
| B | VAL117 |
| B | ASP118 |
| B | ILE119 |
| B | ASP120 |
| B | VAL123 |
| B | ASP149 |
| B | GLY150 |
| B | ASP168 |
| B | THR169 |
| B | THR170 |
| B | PRO175 |
| B | ALA176 |
| B | LEU179 |
| B | TYR237 |
| B | BSX502 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue BSX B 502 |
| Chain | Residue |
| B | TRP19 |
| B | GLN64 |
| B | TYR73 |
| B | THR169 |
| B | THR170 |
| B | ASP171 |
| B | GLN201 |
| B | TYR237 |
| B | PRO238 |
| B | S4M501 |
| B | HOH633 |
| B | HOH660 |
| B | HOH681 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue S4M C 501 |
| Chain | Residue |
| C | GLN40 |
| C | LEU59 |
| C | GLN64 |
| C | HIS74 |
| C | GLY95 |
| C | ASP98 |
| C | ASP118 |
| C | ILE119 |
| C | ASP120 |
| C | VAL123 |
| C | ASP149 |
| C | GLY150 |
| C | ASP168 |
| C | THR169 |
| C | THR170 |
| C | PRO175 |
| C | ALA176 |
| C | LEU179 |
| C | TYR237 |
| C | BSX502 |
| C | HOH626 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue BSX C 502 |
| Chain | Residue |
| C | PRO238 |
| C | S4M501 |
| C | HOH619 |
| C | HOH625 |
| C | HOH679 |
| C | TRP19 |
| C | GLN64 |
| C | TYR73 |
| C | ASP168 |
| C | THR169 |
| C | THR170 |
| C | ASP171 |
| C | GLN201 |
| C | TYR237 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue S4M D 501 |
| Chain | Residue |
| D | GLN40 |
| D | LEU59 |
| D | GLN64 |
| D | TYR73 |
| D | HIS74 |
| D | GLY95 |
| D | ASP98 |
| D | VAL117 |
| D | ASP118 |
| D | ILE119 |
| D | ASP120 |
| D | VAL123 |
| D | ASP149 |
| D | GLY150 |
| D | ASP168 |
| D | THR169 |
| D | THR170 |
| D | PRO175 |
| D | ALA176 |
| D | LEU179 |
| D | TYR237 |
| D | BSX502 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue BSX D 502 |
| Chain | Residue |
| D | TRP19 |
| D | GLN64 |
| D | TYR73 |
| D | THR169 |
| D | THR170 |
| D | ASP171 |
| D | GLN201 |
| D | TYR237 |
| D | PRO238 |
| D | S4M501 |
| D | HOH614 |
| D | HOH637 |
| D | HOH664 |
Functional Information from PROSITE/UniProt
| site_id | PS01330 |
| Number of Residues | 14 |
| Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLIIGGGdGgvLrE |
| Chain | Residue | Details |
| A | VAL91-GLU104 | |
