2D3Q
Crystal Structure of a Decolorizing Peroxidase (DyP) That Catalyses the Biological Oxidation of Anthraquinone Derivatives
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005829 | cellular_component | cytosol |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005829 | cellular_component | cytosol |
B | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM A 446 |
Chain | Residue |
A | GLU165 |
A | HIS308 |
A | THR312 |
A | ASN313 |
A | ARG315 |
A | ARG329 |
A | PHE356 |
A | GLU358 |
A | PHE367 |
A | GLN370 |
A | GLN371 |
A | LEU170 |
A | ILE394 |
A | VAL420 |
A | ASP171 |
A | GLY172 |
A | ILE173 |
A | SER174 |
A | PHE223 |
A | GLN225 |
A | ARG263 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 446 |
Chain | Residue |
B | GLU165 |
B | PHE169 |
B | LEU170 |
B | ASP171 |
B | GLY172 |
B | ILE173 |
B | SER174 |
B | PHE223 |
B | GLN225 |
B | PHE261 |
B | ARG263 |
B | HIS308 |
B | VAL309 |
B | THR312 |
B | ASN313 |
B | ARG315 |
B | ARG329 |
B | PHE356 |
B | PHE367 |
B | GLN370 |
B | GLN371 |
B | ILE394 |
B | VAL420 |