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 | 14 |
Details | binding site for residue OHZ A 601 |
Chain | Residue |
A | ASP167 |
A | TYR422 |
A | SER451 |
A | LEU453 |
A | LEU487 |
A | FAD602 |
A | GLU281 |
A | VAL369 |
A | GLU372 |
A | LEU376 |
A | TRP382 |
A | ASN390 |
A | ILE418 |
A | LEU420 |
site_id | AC2 |
Number of Residues | 31 |
Details | binding site for residue FAD A 602 |
Chain | Residue |
A | PHE60 |
A | PRO98 |
A | ARG99 |
A | GLY100 |
A | GLN101 |
A | GLY102 |
A | HIS103 |
A | SER104 |
A | GLN108 |
A | THR166 |
A | ASP167 |
A | TYR168 |
A | LEU171 |
A | THR172 |
A | GLY174 |
A | GLY175 |
A | THR176 |
A | SER178 |
A | ASN179 |
A | GLY181 |
A | ILE182 |
A | GLY228 |
A | GLY231 |
A | VAL232 |
A | ILE233 |
A | TYR486 |
A | SER521 |
A | GLN524 |
A | OHZ601 |
A | HOH924 |
A | HOH994 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue IPA A 603 |
Chain | Residue |
A | THR357 |
A | SER505 |
A | HOH896 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue IPA A 604 |
Chain | Residue |
A | ARG127 |
A | ASN129 |
A | ASP141 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue IPA A 605 |
Chain | Residue |
A | ALA222 |
A | ARG432 |
A | HOH717 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue IPA A 606 |
Chain | Residue |
A | PHE299 |
A | ASP304 |
A | THR357 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue PEG A 607 |
Chain | Residue |
A | GLU137 |
A | HIS197 |
A | GLU198 |
A | ARG237 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue PEG A 608 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue PEG A 609 |
Chain | Residue |
A | MET213 |
A | ASP214 |
A | ASN216 |
A | SER217 |
A | ASP218 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 610 |
Chain | Residue |
A | ALA258 |
A | THR261 |
A | GLU265 |
A | ARG395 |
A | HOH782 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 611 |
Chain | Residue |
A | GLU241 |
A | PRO242 |
A | ASP278 |
A | TYR328 |
A | HOH749 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 612 |
Chain | Residue |
A | THR491 |
A | SER492 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue EDO A 613 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue EDO A 614 |
Chain | Residue |
A | LEU473 |
A | CYS483 |
A | GLN485 |
A | TYR490 |
A | HOH734 |
A | HOH787 |
A | HOH858 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 615 |
Chain | Residue |
A | MET208 |
A | VAL209 |
A | THR210 |
A | HOH1031 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 616 |
Chain | Residue |
A | ARG374 |
A | ASP400 |
A | ASP403 |
A | GLY404 |
A | PHE475 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue EDO A 617 |
Chain | Residue |
A | HOH817 |
A | HOH920 |
A | PHE527 |
A | PRO528 |
A | HOH726 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 618 |
Chain | Residue |
A | GLN493 |
A | ARG497 |
A | TRP504 |
A | ALA508 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue EDO A 619 |
Chain | Residue |
A | ASP141 |
A | ARG235 |
A | HOH770 |
Functional Information from PROSITE/UniProt
site_id | PS00862 |
Number of Residues | 36 |
Details | OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PeavfhpaTpaDIaalVrfsatsaapfp.VaprGQGH |
Chain | Residue | Details |
A | PRO68-HIS103 | |