4BLZ
CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM VI
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 |
| B | 0000302 | biological_process | response to reactive oxygen species |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016689 | molecular_function | manganese peroxidase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0046274 | biological_process | lignin catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052750 | molecular_function | reactive-black-5:hydrogen-peroxide oxidoreductase activity |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 400 |
| Chain | Residue |
| A | SER171 |
| A | ASP188 |
| A | THR190 |
| A | VAL193 |
| A | ASP195 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | HOH2064 |
| A | HOH2072 |
| A | ASP49 |
| A | GLY61 |
| A | ASP63 |
| A | SER65 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | HIS40 |
| A | GLU41 |
| A | LEU43 |
| A | ARG44 |
| A | PHE47 |
| A | PRO140 |
| A | GLU141 |
| A | PRO142 |
| A | LEU167 |
| A | SER169 |
| A | HIS170 |
| A | ALA173 |
| A | ALA174 |
| A | ALA175 |
| A | ASP176 |
| A | LYS177 |
| A | VAL178 |
| A | PHE187 |
| A | LEU229 |
| A | HOH2049 |
| A | HOH2052 |
| A | HOH2057 |
| A | HOH2058 |
| A | HOH2059 |
| A | HOH2066 |
| A | HOH2211 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 400 |
| Chain | Residue |
| B | SER171 |
| B | ASP188 |
| B | THR190 |
| B | VAL193 |
| B | ASP195 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | ASP49 |
| B | GLY61 |
| B | ASP63 |
| B | SER65 |
| B | HOH2061 |
| B | HOH2066 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | HIS40 |
| B | GLU41 |
| B | LEU43 |
| B | ARG44 |
| B | PHE47 |
| B | GLU141 |
| B | PRO142 |
| B | LEU167 |
| B | SER169 |
| B | HIS170 |
| B | ALA173 |
| B | ALA174 |
| B | ALA175 |
| B | ASP176 |
| B | LYS177 |
| B | VAL178 |
| B | PHE187 |
| B | LEU229 |
| B | SER231 |
| B | HOH2052 |
| B | HOH2057 |
| B | HOH2058 |
| B | HOH2062 |
| B | HOH2218 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tryptophan radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
