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 | 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 | 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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012 |
Chain | Residue | Details |
A | HIS48 | |
B | HIS48 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Tryptophan radical intermediate => ECO:0000250 |
Chain | Residue | Details |
A | TRP165 | |
B | TRP165 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU37 | |
A | GLU41 | |
A | ALA174 | |
A | ASP176 | |
B | GLU37 | |
B | GLU41 | |
B | ALA174 | |
B | ASP176 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00297 |
Chain | Residue | Details |
A | ASP49 | |
B | ASP49 | |
B | GLY61 | |
B | ASP63 | |
B | SER65 | |
B | SER171 | |
B | ASP188 | |
B | THR190 | |
B | VAL193 | |
B | ASP195 | |
A | GLY61 | |
A | ASP63 | |
A | SER65 | |
A | SER171 | |
A | ASP188 | |
A | THR190 | |
A | VAL193 | |
A | ASP195 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00297 |
Chain | Residue | Details |
A | HIS170 | |
B | HIS170 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00297 |
Chain | Residue | Details |
A | ARG44 | |
B | ARG44 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN97 | |
B | ASN97 |