Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| B | 0003824 | molecular_function | catalytic activity |
| C | 0003824 | molecular_function | catalytic activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue GXQ A 401 |
| Chain | Residue |
| A | TRP51 |
| A | GLN229 |
| A | GLU231 |
| A | TYR264 |
| A | MTA402 |
| A | HOH550 |
| A | ILE92 |
| A | GLN93 |
| A | TYR102 |
| A | HIS103 |
| A | ASP127 |
| A | ASP196 |
| A | SER197 |
| A | ASP199 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue MTA A 402 |
| Chain | Residue |
| A | GLN72 |
| A | GLN93 |
| A | GLY124 |
| A | GLY125 |
| A | ASP127 |
| A | CYS146 |
| A | GLU147 |
| A | ILE148 |
| A | VAL152 |
| A | ASP178 |
| A | ALA179 |
| A | ASP196 |
| A | SER198 |
| A | PRO203 |
| A | ALA204 |
| A | THR206 |
| A | LEU207 |
| A | GXQ401 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue 1PG A 403 |
| Chain | Residue |
| A | TRP43 |
| A | TRP43 |
| A | SER45 |
| A | SER45 |
| A | PHE47 |
| A | PHE47 |
| A | SER57 |
| A | HOH511 |
| A | HOH511 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | LYS97 |
| A | PHE100 |
| A | TRP234 |
| A | HOH577 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue GXQ B 401 |
| Chain | Residue |
| B | ILE92 |
| B | GLN93 |
| B | TYR102 |
| B | HIS103 |
| B | ASP127 |
| B | ASP196 |
| B | SER197 |
| B | ASP199 |
| B | GLU231 |
| B | SER232 |
| B | TYR264 |
| B | ILE269 |
| B | MTA402 |
| B | HOH503 |
| B | HOH559 |
| B | HOH577 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue MTA B 402 |
| Chain | Residue |
| B | GLN72 |
| B | GLY124 |
| B | GLY125 |
| B | ASP127 |
| B | CYS146 |
| B | GLU147 |
| B | ILE148 |
| B | VAL152 |
| B | GLU177 |
| B | ASP178 |
| B | ALA179 |
| B | ASP196 |
| B | SER197 |
| B | SER198 |
| B | PRO203 |
| B | ALA204 |
| B | THR206 |
| B | LEU207 |
| B | GXQ401 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | LYS97 |
| B | LYS297 |
| B | HOH543 |
| B | HOH565 |
| B | HOH575 |
| C | TRP234 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue 1PG B 404 |
| Chain | Residue |
| B | PHE47 |
| B | SER57 |
| C | TRP43 |
| C | PHE47 |
| C | SER57 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| B | LYS286 |
| B | LYS287 |
| B | GLU289 |
| B | SER290 |
| B | PHE293 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | LYS291 |
| B | HIS236 |
| B | VAL237 |
| B | GLY238 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue JFQ C 401 |
| Chain | Residue |
| C | ILE92 |
| C | GLN93 |
| C | TYR102 |
| C | HIS103 |
| C | ASP127 |
| C | ASP196 |
| C | SER197 |
| C | ASP199 |
| C | GLN229 |
| C | TYR264 |
| C | ILE269 |
| C | MTA402 |
| C | HOH562 |
| C | HOH594 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for residue MTA C 402 |
| Chain | Residue |
| C | GLN72 |
| C | GLN93 |
| C | GLY124 |
| C | GLY125 |
| C | ASP127 |
| C | CYS146 |
| C | GLU147 |
| C | ILE148 |
| C | ASP149 |
| C | VAL152 |
| C | GLU177 |
| C | ASP178 |
| C | ALA179 |
| C | ASP196 |
| C | SER197 |
| C | SER198 |
| C | PRO203 |
| C | ALA204 |
| C | THR206 |
| C | LEU207 |
| C | JFQ401 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| B | TRP234 |
| C | LYS97 |
| C | LYS297 |
| C | HOH522 |
| C | HOH549 |
| C | HOH584 |
| C | HOH598 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | PHE208 |
| C | THR239 |
| C | ASN242 |
| C | TYR246 |
| C | HOH645 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL C 405 |
| Chain | Residue |
| B | PHE56 |
| B | PRO262 |
| B | CYS266 |
| C | PRO262 |
| C | PRO265 |
| C | CYS266 |
| C | GLY267 |
| C | HOH540 |
| C | HOH629 |
| C | HOH639 |
Functional Information from PROSITE/UniProt
| site_id | PS01330 |
| Number of Residues | 14 |
| Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLVVGGGdGgiIrE |
| Chain | Residue | Details |
| A | VAL120-GLU133 | |
