Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016688 | molecular_function | L-ascorbate peroxidase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016688 | molecular_function | L-ascorbate peroxidase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| 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 | 20 |
| Details | binding site for residue HEM A 301 |
| Chain | Residue |
| A | PRO34 |
| A | ALA168 |
| A | HIS169 |
| A | ARG172 |
| A | SER173 |
| A | TRP179 |
| A | SER207 |
| A | TYR235 |
| A | HOH410 |
| A | HOH428 |
| A | HOH442 |
| A | PHE41 |
| A | HOH517 |
| A | PRO132 |
| A | PRO134 |
| A | PHE145 |
| A | LEU159 |
| A | MHS163 |
| A | GLY166 |
| A | ALA167 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | LYS20 |
| A | ARG24 |
| A | LYS112 |
| A | HOH404 |
| A | HOH493 |
| B | LYS112 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | GLY137 |
| A | SER138 |
| A | ASP139 |
| A | HIS140 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | ARG31 |
| A | LEU184 |
| A | HOH494 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue HEM B 301 |
| Chain | Residue |
| B | PRO34 |
| B | ARG38 |
| B | PHE41 |
| B | PRO132 |
| B | PRO134 |
| B | PHE145 |
| B | LEU159 |
| B | MHS163 |
| B | GLY166 |
| B | ALA167 |
| B | ALA168 |
| B | HIS169 |
| B | ARG172 |
| B | SER173 |
| B | TRP179 |
| B | SER207 |
| B | TYR235 |
| B | HOH431 |
| B | HOH433 |
| B | HOH443 |
| B | HOH484 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| A | LYS112 |
| B | LYS20 |
| B | ARG24 |
| B | LYS112 |
| B | HOH418 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | LYS136 |
| B | GLY137 |
| B | SER138 |
| B | ASP139 |
| B | HIS140 |
| B | HOH506 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 304 |
| Chain | Residue |
| B | ARG31 |
| B | HOH485 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIVALSGGHTI |
| Chain | Residue | Details |
| A | ASP155-ILE165 | |
| site_id | PS00436 |
| Number of Residues | 12 |
| Details | PEROXIDASE_2 Peroxidases active site signature. APlmLRLaFHSA |
| Chain | Residue | Details |
| A | ALA33-ALA44 | |
