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 | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 350 |
| Chain | Residue |
| A | HIS39 |
| A | LEU166 |
| A | SER168 |
| A | HIS169 |
| A | ALA172 |
| A | ALA173 |
| A | ALA174 |
| A | ALA175 |
| A | LYS176 |
| A | VAL177 |
| A | PHE186 |
| A | GLU40 |
| A | LEU228 |
| A | SER230 |
| A | HOH385 |
| A | HOH510 |
| A | HOH631 |
| A | HOH690 |
| A | LEU42 |
| A | ARG43 |
| A | PHE46 |
| A | PRO139 |
| A | GLU140 |
| A | PRO141 |
| A | LEU165 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 351 |
| Chain | Residue |
| A | ASP48 |
| A | GLY60 |
| A | ASP62 |
| A | SER64 |
| A | HOH342 |
| A | HOH456 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 352 |
| Chain | Residue |
| A | SER170 |
| A | ASP187 |
| A | THR189 |
| A | VAL192 |
| A | ASP194 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 332 |
| Chain | Residue |
| A | ASP30 |
| A | GLU37 |
| A | HIS232 |
| A | ARG236 |
| A | HOH432 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 333 |
| Chain | Residue |
| A | GLU26 |
| A | ASP237 |
| A | HOH345 |
| A | HOH499 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 334 |
| Chain | Residue |
| A | GLU140 |
| A | ASP143 |
| A | CAC340 |
| A | CAC341 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE A 335 |
| Chain | Residue |
| A | HIS293 |
| A | ASP318 |
| A | HOH647 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 336 |
| Chain | Residue |
| A | HIS95 |
| A | HOH497 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 337 |
| Chain | Residue |
| A | HIS136 |
| A | CAC340 |
| A | CAC341 |
| A | HOH469 |
| A | HOH593 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 338 |
| Chain | Residue |
| A | GLU36 |
| A | GLU40 |
| A | GLU83 |
| A | GLN219 |
| A | HOH563 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 339 |
| Chain | Residue |
| A | ASP69 |
| A | LYS89 |
| A | HOH366 |
| A | HOH447 |
| A | HOH583 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CAC A 340 |
| Chain | Residue |
| A | HIS136 |
| A | VAL138 |
| A | GLU140 |
| A | ASP143 |
| A | ZN334 |
| A | ZN337 |
| A | CAC341 |
| A | HOH375 |
| A | HOH469 |
| A | HOH519 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CAC A 341 |
| Chain | Residue |
| A | HIS136 |
| A | GLU140 |
| A | ASP143 |
| A | ZN334 |
| A | ZN337 |
| A | CAC340 |
| A | HOH373 |
| A | HOH469 |
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 | GLU161-ILE171 | |
| site_id | PS00436 |
| Number of Residues | 12 |
| Details | PEROXIDASE_2 Peroxidases active site signature. VHesLRLtFHDA |
| Chain | Residue | Details |
| A | VAL38-ALA49 | |
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":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| A | HIS47 | |
| A | ARG43 | |
| A | ASN78 | |
