Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005773 | cellular_component | vacuole |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140825 | molecular_function | lactoperoxidase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005773 | cellular_component | vacuole |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0140825 | molecular_function | lactoperoxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 351 |
| Chain | Residue |
| A | THR171 |
| A | ASP222 |
| A | THR225 |
| A | ILE228 |
| A | ASP230 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 352 |
| Chain | Residue |
| A | ASP43 |
| A | VAL46 |
| A | GLY48 |
| A | ASP50 |
| A | SER52 |
| A | HOH721 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 351 |
| Chain | Residue |
| B | THR171 |
| B | ASP222 |
| B | THR225 |
| B | ILE228 |
| B | ASP230 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 352 |
| Chain | Residue |
| B | ASP43 |
| B | VAL46 |
| B | GLY48 |
| B | ASP50 |
| B | SER52 |
| B | HOH721 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 350 |
| Chain | Residue |
| A | ARG31 |
| A | ALA34 |
| A | SER35 |
| A | ARG38 |
| A | PHE41 |
| A | SER73 |
| A | PRO139 |
| A | ALA140 |
| A | PRO141 |
| A | LEU166 |
| A | GLY169 |
| A | HIS170 |
| A | PHE172 |
| A | GLY173 |
| A | LYS174 |
| A | ASN175 |
| A | GLN176 |
| A | PHE179 |
| A | PHE221 |
| A | SER246 |
| A | BHO353 |
| A | HOH768 |
| A | HOH803 |
| A | HOH999 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BHO A 353 |
| Chain | Residue |
| A | ARG38 |
| A | PHE41 |
| A | HIS42 |
| A | PHE68 |
| A | GLY69 |
| A | PRO139 |
| A | PHE179 |
| A | HEM350 |
| A | HOH999 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B 350 |
| Chain | Residue |
| B | ARG31 |
| B | ALA34 |
| B | SER35 |
| B | ARG38 |
| B | PHE41 |
| B | SER73 |
| B | PRO139 |
| B | ALA140 |
| B | PRO141 |
| B | LEU166 |
| B | GLY169 |
| B | HIS170 |
| B | PHE172 |
| B | GLY173 |
| B | LYS174 |
| B | ASN175 |
| B | GLN176 |
| B | PHE179 |
| B | PHE221 |
| B | SER246 |
| B | BHO353 |
| B | HOH768 |
| B | HOH803 |
| B | HOH999 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BHO B 353 |
| Chain | Residue |
| B | GLY69 |
| B | PRO139 |
| B | PHE179 |
| B | HEM350 |
| B | HOH999 |
| B | ARG38 |
| B | PHE41 |
| B | HIS42 |
| B | PHE68 |
| site_id | BEM |
| Number of Residues | 8 |
| Details | BENZHYDROZAMIC ACID BINDING SITE. |
| Chain | Residue |
| B | HIS42 |
| B | PHE68 |
| B | GLY69 |
| B | PRO139 |
| B | ALA140 |
| B | PRO141 |
| B | PHE179 |
| B | ARG38 |
| site_id | BEN |
| Number of Residues | 8 |
| Details | BENZHYDROZAMIC ACID BINDING SITE. |
| Chain | Residue |
| A | ARG38 |
| A | HIS42 |
| A | PHE68 |
| A | GLY69 |
| A | PRO139 |
| A | ALA140 |
| A | PRO141 |
| A | PHE179 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DLVALSGGHTF |
| Chain | Residue | Details |
| A | ASP162-PHE172 | |
| site_id | PS00436 |
| Number of Residues | 12 |
| Details | PEROXIDASE_2 Peroxidases active site signature. AAsiLRLhFHDC |
| Chain | Residue | Details |
| A | ALA33-CYS44 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS42 | |
| B | HIS42 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP43 | |
| A | THR225 | |
| A | ASP230 | |
| B | ASP43 | |
| B | VAL46 | |
| B | GLY48 | |
| B | ASP50 | |
| B | SER52 | |
| B | GLU64 | |
| B | PRO139 | |
| B | THR171 | |
| A | VAL46 | |
| B | ASP222 | |
| B | THR225 | |
| B | ASP230 | |
| A | GLY48 | |
| A | ASP50 | |
| A | SER52 | |
| A | GLU64 | |
| A | PRO139 | |
| A | THR171 | |
| A | ASP222 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | HIS170 | |
| B | HIS170 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG38 | |
| B | ARG38 | |
| Chain | Residue | Details |
| A | GLN1 | |
| B | GLN1 | |
| Chain | Residue | Details |
| A | ASN13 | |
| A | ASN57 | |
| B | ASN13 | |
| B | ASN57 | |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | ASN158 | |
| B | ASN214 | |
| B | ASN255 | |
| B | ASN268 | |
| A | ASN186 | |
| A | ASN198 | |
| A | ASN214 | |
| A | ASN255 | |
| A | ASN268 | |
| B | ASN158 | |
| B | ASN186 | |
| B | ASN198 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 239 |
| Chain | Residue | Details |
| A | ARG38 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS42 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN70 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| A | HIS170 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 239 |
| Chain | Residue | Details |
| B | ARG38 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS42 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN70 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| B | HIS170 | metal ligand |
