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 |