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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 601 |
Chain | Residue |
A | SER261 |
A | THR264 |
A | ALA265 |
A | GLU268 |
A | ARG404 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 602 |
Chain | Residue |
A | ASP221 |
A | ARG435 |
A | HOH847 |
site_id | AC3 |
Number of Residues | 32 |
Details | binding site for residue FAD A 603 |
Chain | Residue |
A | ALA95 |
A | ARG96 |
A | GLY97 |
A | HIS98 |
A | GLY99 |
A | HIS100 |
A | SER101 |
A | GLN105 |
A | ALA106 |
A | THR169 |
A | ASP170 |
A | TYR171 |
A | LEU174 |
A | SER175 |
A | GLY177 |
A | GLY178 |
A | SER181 |
A | ASN182 |
A | GLY184 |
A | ILE185 |
A | GLY234 |
A | ILE235 |
A | ILE236 |
A | TRP389 |
A | TYR487 |
A | GLN526 |
A | OHZ604 |
A | HOH719 |
A | HOH810 |
A | HOH842 |
A | HOH844 |
A | PHE57 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue OHZ A 604 |
Chain | Residue |
A | ASP170 |
A | GLU285 |
A | VAL370 |
A | LEU377 |
A | TRP383 |
A | TRP389 |
A | ASN391 |
A | LEU423 |
A | TYR425 |
A | LEU448 |
A | LEU452 |
A | FAD603 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue DMS A 605 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue DMS A 606 |
Chain | Residue |
A | HIS430 |
A | LYS431 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue DMS A 607 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO A 608 |
Chain | Residue |
A | TRP252 |
A | THR359 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO A 609 |
Chain | Residue |
A | ASN219 |
A | PRO220 |
A | ASP221 |
A | LEU222 |
A | PHE516 |
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 | |