4ML8
Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0009690 | biological_process | cytokinin metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019139 | molecular_function | cytokinin dehydrogenase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009690 | biological_process | cytokinin metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019139 | molecular_function | cytokinin dehydrogenase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD A 601 |
| Chain | Residue |
| A | PHE55 |
| A | THR157 |
| A | ASP158 |
| A | TYR159 |
| A | LEU162 |
| A | THR163 |
| A | GLY165 |
| A | GLY166 |
| A | THR167 |
| A | SER169 |
| A | ASN170 |
| A | ALA95 |
| A | GLY172 |
| A | VAL173 |
| A | GLY219 |
| A | GLY222 |
| A | ILE223 |
| A | ILE224 |
| A | TRP373 |
| A | TYR469 |
| A | GLN507 |
| A | GLY97 |
| A | HIS98 |
| A | GLY99 |
| A | HIS100 |
| A | SER101 |
| A | GLN105 |
| A | SER106 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG A 602 |
| Chain | Residue |
| A | ARG53 |
| A | ARG96 |
| A | HIS98 |
| A | GLY99 |
| A | HIS100 |
| A | TYR159 |
| A | TRP367 |
| A | GLU368 |
| A | HOH727 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD B 601 |
| Chain | Residue |
| B | PHE55 |
| B | ALA95 |
| B | GLY97 |
| B | HIS98 |
| B | GLY99 |
| B | HIS100 |
| B | SER101 |
| B | GLN105 |
| B | SER106 |
| B | THR157 |
| B | ASP158 |
| B | TYR159 |
| B | THR163 |
| B | GLY166 |
| B | THR167 |
| B | SER169 |
| B | ASN170 |
| B | GLY172 |
| B | VAL173 |
| B | GLY219 |
| B | GLY222 |
| B | ILE223 |
| B | ILE224 |
| B | TRP373 |
| B | TYR469 |
| B | GLN507 |
| B | HOH721 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD C 601 |
| Chain | Residue |
| C | PHE55 |
| C | ALA95 |
| C | GLY97 |
| C | HIS98 |
| C | GLY99 |
| C | HIS100 |
| C | SER101 |
| C | GLN105 |
| C | SER106 |
| C | THR157 |
| C | ASP158 |
| C | TYR159 |
| C | LEU162 |
| C | THR163 |
| C | GLY165 |
| C | GLY166 |
| C | THR167 |
| C | SER169 |
| C | ASN170 |
| C | GLY172 |
| C | VAL173 |
| C | GLY219 |
| C | GLY222 |
| C | ILE223 |
| C | ILE224 |
| C | TRP373 |
| C | TYR469 |
| C | GLN507 |
| C | HOH719 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD D 601 |
| Chain | Residue |
| D | SER101 |
| D | GLN105 |
| D | SER106 |
| D | THR157 |
| D | ASP158 |
| D | TYR159 |
| D | LEU162 |
| D | THR163 |
| D | GLY166 |
| D | THR167 |
| D | SER169 |
| D | ASN170 |
| D | GLY172 |
| D | VAL173 |
| D | GLY219 |
| D | GLY222 |
| D | ILE223 |
| D | ILE224 |
| D | TRP373 |
| D | TYR469 |
| D | GLN507 |
| D | PHE55 |
| D | ALA95 |
| D | GLY97 |
| D | HIS98 |
| D | GLY99 |
| D | HIS100 |
Functional Information from PROSITE/UniProt
| site_id | PS00862 |
| Number of Residues | 36 |
| Details | OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PaavlhpgSvsDIaatVrhvfslgegsp.LtvaARGH |
| Chain | Residue | Details |
| A | PRO63-HIS98 |
