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 | 28 |
| Details | BINDING SITE FOR RESIDUE HEM A 350 |
| Chain | Residue |
| A | ARG31 |
| A | PRO141 |
| A | LEU148 |
| A | PHE152 |
| A | LEU166 |
| A | TYR167 |
| A | GLY169 |
| A | HIS170 |
| A | GLY173 |
| A | LYS174 |
| A | ASN175 |
| A | ALA34 |
| A | GLN176 |
| A | PHE179 |
| A | PHE221 |
| A | ILE244 |
| A | SER246 |
| A | ACT1309 |
| A | HOH2084 |
| A | HOH2090 |
| A | HOH2091 |
| A | SER35 |
| A | ARG38 |
| A | PHE41 |
| A | SER73 |
| A | ARG75 |
| A | PRO139 |
| A | ALA140 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1307 |
| Chain | Residue |
| A | ASP43 |
| A | VAL46 |
| A | GLY48 |
| A | ASP50 |
| A | SER52 |
| A | HOH2101 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1308 |
| Chain | Residue |
| A | THR171 |
| A | ASP222 |
| A | THR225 |
| A | ILE228 |
| A | ASP230 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 1309 |
| Chain | Residue |
| A | ARG38 |
| A | PHE41 |
| A | HIS42 |
| A | LEU138 |
| A | PRO139 |
| A | HEM350 |
| A | HOH2090 |
| A | HOH2257 |
| A | HOH2431 |
Functional Information from PROSITE/UniProt
| 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 | 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 |
