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 | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA A 401 | 
| Chain | Residue | 
| A | ASP43 | 
| A | VAL46 | 
| A | GLY48 | 
| A | ASP50 | 
| A | SER52 | 
| A | HOH2118 | 
| site_id | AC2 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CA A 402 | 
| Chain | Residue | 
| A | ILE228 | 
| A | ASP230 | 
| A | THR171 | 
| A | ASP222 | 
| A | THR225 | 
| site_id | AC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ACT A 501 | 
| Chain | Residue | 
| A | ARG38 | 
| A | PHE41 | 
| A | HIS42 | 
| A | PRO139 | 
| A | HEM350 | 
| site_id | AC4 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE ACT A 502 | 
| Chain | Residue | 
| A | LYS65 | 
| A | PHE77 | 
| A | ARG302 | 
| site_id | AC5 | 
| Number of Residues | 26 | 
| 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 | PHE152 | 
| A | LEU166 | 
| A | SER167 | 
| A | GLY169 | 
| A | HIS170 | 
| A | PHE172 | 
| A | GLY173 | 
| A | LYS174 | 
| A | ASN175 | 
| A | GLN176 | 
| A | PHE179 | 
| A | PHE221 | 
| A | SER246 | 
| A | ACT501 | 
| A | HOH2258 | 
| A | HOH2403 | 
| A | HOH2404 | 
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 | 1 | 
| Details | Active site: {"description":"Proton acceptor"} | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 11 | 
| Details | Binding site: {} | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 1 | 
| Details | Binding site: {"description":"axial binding residue"} | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 1 | 
| Details | Site: {"description":"Transition state stabilizer"} | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1001465","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 2 | 
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1001465","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI7 | 
| Number of Residues | 6 | 
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 7atj | 
| Chain | Residue | Details | 
| A | ARG38 |  | 
| A | HIS42 |  | 
| A | ASN70 |  | 
| 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 |