Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000302 | biological_process | response to reactive oxygen species |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006979 | biological_process | response to oxidative stress |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016689 | molecular_function | manganese peroxidase activity |
A | 0020037 | molecular_function | heme binding |
A | 0034599 | biological_process | cellular response to oxidative stress |
A | 0042744 | biological_process | hydrogen peroxide catabolic process |
A | 0046274 | biological_process | lignin catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0052750 | molecular_function | reactive-black-5:hydrogen-peroxide oxidoreductase activity |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 400 |
Chain | Residue |
A | ASP49 |
A | GLY61 |
A | ASP63 |
A | SER65 |
A | HOH2094 |
A | HOH2102 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 401 |
Chain | Residue |
A | VAL193 |
A | ASP195 |
A | SER171 |
A | ASP188 |
A | THR190 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM A 500 |
Chain | Residue |
A | HIS40 |
A | GLU41 |
A | LEU43 |
A | ARG44 |
A | PHE47 |
A | GLU141 |
A | PRO142 |
A | LEU166 |
A | LEU167 |
A | SER169 |
A | HIS170 |
A | ALA173 |
A | ALA174 |
A | ALA175 |
A | ASP176 |
A | LYS177 |
A | VAL178 |
A | PHE187 |
A | LEU229 |
A | SER231 |
A | HOH2075 |
A | HOH2077 |
A | HOH2078 |
A | HOH2088 |
A | HOH2282 |
Functional Information from PROSITE/UniProt
site_id | PS00435 |
Number of Residues | 11 |
Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVWLLASHSI |
Chain | Residue | Details |
A | GLU162-ILE172 | |
site_id | PS00436 |
Number of Residues | 12 |
Details | PEROXIDASE_2 Peroxidases active site signature. VHesLRLtFHDA |
Chain | Residue | Details |
A | VAL39-ALA50 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Tryptophan radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |