Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0004601 | molecular_function | peroxidase activity |
X | 0006979 | biological_process | response to oxidative stress |
X | 0016688 | molecular_function | L-ascorbate peroxidase activity |
X | 0020037 | molecular_function | heme binding |
X | 0034599 | biological_process | cellular response to oxidative stress |
X | 0046872 | molecular_function | metal ion binding |
X | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA X 252 |
Chain | Residue |
X | THR164 |
X | THR180 |
X | ASN182 |
X | ILE185 |
X | HOH2319 |
X | HOH2324 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM X 251 |
Chain | Residue |
X | ALA134 |
X | LEU159 |
X | SER160 |
X | GLY162 |
X | HIS163 |
X | ILE165 |
X | GLY166 |
X | ALA167 |
X | ALA168 |
X | HIS169 |
X | ARG172 |
X | SER173 |
X | TRP179 |
X | LEU205 |
X | SER207 |
X | TYR235 |
X | SHA253 |
X | HOH2401 |
X | HOH2402 |
X | HOH2403 |
X | PRO34 |
X | TRP41 |
X | PRO132 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SHA X 253 |
Chain | Residue |
X | ARG38 |
X | TRP41 |
X | HIS42 |
X | ALA70 |
X | PRO132 |
X | HEM251 |
Functional Information from PROSITE/UniProt
site_id | PS00435 |
Number of Residues | 11 |
Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIVALSGGHTI |
Chain | Residue | Details |
X | ASP155-ILE165 | |
site_id | PS00436 |
Number of Residues | 12 |
Details | PEROXIDASE_2 Peroxidases active site signature. APlmLRLaWHSA |
Chain | Residue | Details |
X | ALA33-ALA44 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
X | ARG38 | |
X | HIS42 | |
X | ASN71 | |