Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
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 |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0006979 | biological_process | response to oxidative stress |
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 | 6 |
Details | BINDING SITE FOR RESIDUE CA A 2001 |
Chain | Residue |
A | ASP43 |
A | VAL46 |
A | GLY48 |
A | ASP50 |
A | SER52 |
A | HOH2012 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 2002 |
Chain | Residue |
A | THR223 |
A | ASP225 |
A | THR166 |
A | ASP217 |
A | THR220 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 2001 |
Chain | Residue |
B | ASP43 |
B | VAL46 |
B | GLY48 |
B | ASP50 |
B | SER52 |
B | HOH2335 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 2002 |
Chain | Residue |
B | THR166 |
B | ASP217 |
B | THR220 |
B | THR223 |
B | ASP225 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 1350 |
Chain | Residue |
A | ARG31 |
A | ALA34 |
A | SER35 |
A | ARG38 |
A | PHE41 |
A | SER70 |
A | ARG72 |
A | PRO135 |
A | SER136 |
A | PRO137 |
A | LEU161 |
A | SER162 |
A | ALA164 |
A | HIS165 |
A | PHE167 |
A | GLY168 |
A | GLN169 |
A | ALA170 |
A | LYS171 |
A | SER241 |
A | HOH2049 |
A | HOH2065 |
A | HOH2171 |
A | HOH2525 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 1350 |
Chain | Residue |
B | ARG31 |
B | ALA34 |
B | SER35 |
B | ARG38 |
B | PHE41 |
B | SER70 |
B | ARG72 |
B | PRO135 |
B | SER136 |
B | PRO137 |
B | LEU161 |
B | SER162 |
B | ALA164 |
B | HIS165 |
B | PHE167 |
B | GLY168 |
B | GLN169 |
B | ALA170 |
B | LYS171 |
B | SER241 |
B | HOH2023 |
B | HOH2122 |
B | HOH2530 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GSH A 1794 |
Chain | Residue |
A | ASN154 |
A | THR156 |
A | ASP157 |
A | CYS275 |
A | ALA276 |
A | ARG279 |
B | LYS27 |
B | ALA28 |
B | HOH2292 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GSH B 1794 |
Chain | Residue |
B | THR156 |
B | ASP157 |
B | CYS275 |
B | ALA276 |
B | ARG279 |
B | HOH2177 |
B | HOH2238 |
B | HOH2322 |
Functional Information from PROSITE/UniProt
site_id | PS00435 |
Number of Residues | 11 |
Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DVVALSGAHTF |
Chain | Residue | Details |
A | ASP157-PHE167 | |
site_id | PS00436 |
Number of Residues | 12 |
Details | PEROXIDASE_2 Peroxidases active site signature. AAslIRLhFHDC |
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 | |
Chain | Residue | Details |
A | ASP43 | |
A | ASP225 | |
B | ASP43 | |
B | VAL46 | |
B | GLY48 | |
B | ASP50 | |
B | SER52 | |
B | THR166 | |
B | ASP217 | |
B | THR220 | |
B | THR223 | |
A | VAL46 | |
B | ASP225 | |
A | GLY48 | |
A | ASP50 | |
A | SER52 | |
A | THR166 | |
A | ASP217 | |
A | THR220 | |
A | THR223 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | PRO135 | |
B | PRO135 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | HIS165 | |
B | HIS165 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG38 | |
B | ARG38 | |
Chain | Residue | Details |
A | GLN1 | |
B | GLN1 | |
site_id | SWS_FT_FI7 |
Number of Residues | 10 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN154 | |
B | ASN282 | |
A | ASN181 | |
A | ASN211 | |
A | ASN253 | |
A | ASN282 | |
B | ASN154 | |
B | ASN181 | |
B | ASN211 | |
B | ASN253 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
A | ARG38 | |
A | HIS42 | |
A | ALA71 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
B | ARG38 | |
B | HIS42 | |
B | ALA71 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
A | ARG38 | |
A | HIS42 | |
A | ASN67 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
B | ARG38 | |
B | HIS42 | |
B | ASN67 | |