Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0009690 | biological_process | cytokinin metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019139 | molecular_function | cytokinin dehydrogenase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 601 |
| Chain | Residue |
| A | PHE57 |
| A | ALA106 |
| A | THR169 |
| A | ASP170 |
| A | TYR171 |
| A | LEU174 |
| A | SER175 |
| A | GLY177 |
| A | GLY178 |
| A | SER181 |
| A | ASN182 |
| A | ALA95 |
| A | GLY184 |
| A | ILE185 |
| A | GLY234 |
| A | ILE235 |
| A | ILE236 |
| A | TRP389 |
| A | TYR487 |
| A | LEU488 |
| A | GLN526 |
| A | 245602 |
| A | ARG96 |
| A | HOH718 |
| A | HOH719 |
| A | HOH746 |
| A | HOH864 |
| A | GLY97 |
| A | HIS98 |
| A | GLY99 |
| A | HIS100 |
| A | SER101 |
| A | GLN105 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 245 A 602 |
| Chain | Residue |
| A | ASP170 |
| A | VAL370 |
| A | TRP389 |
| A | ASN391 |
| A | LEU423 |
| A | LEU452 |
| A | TYR487 |
| A | LEU488 |
| A | FAD601 |
| A | EDO610 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 603 |
| Chain | Residue |
| A | HIS98 |
| A | TYR171 |
| A | HIS371 |
| A | GLU374 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 604 |
| Chain | Residue |
| A | GLY139 |
| A | HIS140 |
| A | LEU243 |
| A | ARG245 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 605 |
| Chain | Residue |
| A | PHE224 |
| A | ARG435 |
| A | SER436 |
| A | SER437 |
| A | ARG505 |
| A | ARG508 |
| A | HOH716 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 606 |
| Chain | Residue |
| A | PHE190 |
| A | HIS191 |
| A | ILE271 |
| A | LEU273 |
| A | ASN428 |
| A | HIS430 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 607 |
| Chain | Residue |
| A | SER159 |
| A | SER397 |
| A | ARG398 |
| A | GLY481 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 608 |
| Chain | Residue |
| A | ALA510 |
| A | ALA514 |
| A | PRO518 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 609 |
| Chain | Residue |
| A | ARG166 |
| A | SER197 |
| A | TYR200 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 610 |
| Chain | Residue |
| A | HIS387 |
| A | TRP389 |
| A | LEU452 |
| A | ARG453 |
| A | SER454 |
| A | 245602 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 611 |
| Chain | Residue |
| A | HIS192 |
| A | SER197 |
| A | LYS431 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 612 |
| Chain | Residue |
| A | ALA129 |
| A | LEU130 |
| A | VAL132 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS A 613 |
| Chain | Residue |
| A | TRP432 |
| A | ALA438 |
| A | THR440 |
| A | HOH783 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 614 |
| Chain | Residue |
| A | ASP152 |
| A | ASN155 |
| A | TYR173 |
| A | GLU444 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 615 |
| Chain | Residue |
| A | LEU474 |
| A | ALA484 |
| A | GLN486 |
| A | HIS491 |
| A | GLU496 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 616 |
| Chain | Residue |
| A | TYR200 |
| A | GLU201 |
| A | THR217 |
| A | ARG240 |
| A | GLU461 |
| A | HOH776 |
Functional Information from PROSITE/UniProt
| site_id | PS00862 |
| Number of Residues | 36 |
| Details | OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PmavfhprAagDVaglVgaafrsargfr.VsarGHGH |
| Chain | Residue | Details |
| A | PRO65-HIS100 | |
