Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009690 | biological_process | cytokinin metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019139 | molecular_function | cytokinin dehydrogenase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| 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 | THR179 |
| A | SER181 |
| A | ALA95 |
| A | ASN182 |
| A | GLY184 |
| A | ILE185 |
| A | GLY234 |
| A | ILE235 |
| A | ILE236 |
| A | TRP389 |
| A | TYR487 |
| A | LEU488 |
| A | GLN526 |
| A | ARG96 |
| A | 245602 |
| A | HOH704 |
| A | HOH710 |
| A | HOH723 |
| A | HOH731 |
| A | HOH736 |
| A | GLY97 |
| A | HIS98 |
| A | GLY99 |
| A | HIS100 |
| A | SER101 |
| A | GLN105 |
| site_id | AC2 |
| Number of Residues | 8 |
| 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 | FAD601 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS A 603 |
| Chain | Residue |
| A | TRP252 |
| A | THR359 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DMS A 604 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DMS A 605 |
| site_id | AC6 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD B 601 |
| Chain | Residue |
| B | PHE57 |
| B | ALA95 |
| B | ARG96 |
| B | GLY97 |
| B | HIS98 |
| B | GLY99 |
| B | HIS100 |
| B | SER101 |
| B | GLN105 |
| B | ALA106 |
| B | THR169 |
| B | ASP170 |
| B | TYR171 |
| B | LEU174 |
| B | SER175 |
| B | GLY177 |
| B | GLY178 |
| B | THR179 |
| B | SER181 |
| B | ASN182 |
| B | GLY184 |
| B | ILE185 |
| B | GLY234 |
| B | ILE235 |
| B | ILE236 |
| B | TRP389 |
| B | TYR487 |
| B | LEU488 |
| B | GLN526 |
| B | 245602 |
| B | HOH706 |
| B | HOH707 |
| B | HOH709 |
| B | HOH714 |
| B | HOH800 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 245 B 602 |
| Chain | Residue |
| B | ASP170 |
| B | VAL370 |
| B | TRP389 |
| B | ASN391 |
| B | LEU423 |
| B | LEU452 |
| B | TYR487 |
| B | FAD601 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS B 603 |
| Chain | Residue |
| B | TRP252 |
| B | THR359 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DMS B 604 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS B 605 |
| Chain | Residue |
| B | ARG238 |
| B | ARG240 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS B 606 |
| Chain | Residue |
| B | PRO518 |
| B | ARG530 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS B 607 |
| Chain | Residue |
| B | ARG72 |
| B | TRP145 |
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 | |
