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 | 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 A1308 |
Chain | Residue |
A | ASP43 |
A | VAL46 |
A | GLY48 |
A | ASP50 |
A | SER52 |
A | HOH2095 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A1309 |
Chain | Residue |
A | ILE228 |
A | ASP230 |
A | THR171 |
A | ASP222 |
A | THR225 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM A1307 |
Chain | Residue |
A | ARG31 |
A | ALA34 |
A | SER35 |
A | ARG38 |
A | PHE41 |
A | SER73 |
A | PRO139 |
A | ALA140 |
A | PRO141 |
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 | CMO1310 |
A | HOH2044 |
A | HOH2340 |
A | HOH2341 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CMO A1310 |
Chain | Residue |
A | ARG38 |
A | PHE41 |
A | HIS42 |
A | HEM1307 |
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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS42 | |
site_id | SWS_FT_FI2 |
Number of Residues | 11 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP43 | |
A | THR225 | |
A | ASP230 | |
A | VAL46 | |
A | GLY48 | |
A | ASP50 | |
A | SER52 | |
A | GLU64 | |
A | PRO139 | |
A | THR171 | |
A | ASP222 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | HIS170 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG38 | |
Chain | Residue | Details |
A | ASN13 | |
A | ASN57 | |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN158 | |
A | ASN186 | |
A | ASN198 | |
A | ASN214 | |
A | ASN255 | |
A | ASN268 | |
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 |