5J92
Crystal structure of a putative alpha-ketoglutarate dependent 2,4-D dioxygenase from Burkholderia xenovorans
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
A | 1901360 | biological_process | organic cyclic compound metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
B | 1901360 | biological_process | organic cyclic compound metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051213 | molecular_function | dioxygenase activity |
C | 1901360 | biological_process | organic cyclic compound metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051213 | molecular_function | dioxygenase activity |
D | 1901360 | biological_process | organic cyclic compound metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue FE2 A 401 |
Chain | Residue |
A | HIS114 |
A | ASP116 |
A | HIS263 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue FE2 B 401 |
Chain | Residue |
B | HIS114 |
B | ASP116 |
B | HIS263 |
B | ARG279 |
B | HOH684 |
B | HOH748 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue FE2 C 401 |
Chain | Residue |
C | HIS114 |
C | ASP116 |
C | HIS263 |
C | ARG279 |
C | HOH562 |
C | HOH700 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ACT C 402 |
Chain | Residue |
C | THR141 |
C | GLY265 |
C | ARG275 |
C | HOH562 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue FE2 D 401 |
Chain | Residue |
D | HIS114 |
D | ASP116 |
D | HIS263 |
D | ARG279 |