5FNB
CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII SEPTUPLE MUTANT E37K, H39R, V160A, T184M, Q202L, D213A & G330R
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 | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | ASP48 |
| A | GLY60 |
| A | ASP62 |
| A | SER64 |
| A | HOH2069 |
| A | HOH2076 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 402 |
| Chain | Residue |
| A | VAL192 |
| A | ASP194 |
| A | SER170 |
| A | ASP187 |
| A | THR189 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | ARG39 |
| A | GLU40 |
| A | LEU42 |
| A | ARG43 |
| A | PHE46 |
| A | GLU140 |
| A | PRO141 |
| A | LEU165 |
| A | LEU166 |
| A | SER168 |
| A | HIS169 |
| A | ALA172 |
| A | ALA173 |
| A | ALA174 |
| A | ASP175 |
| A | LYS176 |
| A | VAL177 |
| A | PHE186 |
| A | LEU228 |
| A | SER230 |
| A | HOH2058 |
| A | HOH2064 |
| A | HOH2065 |
| A | HOH2210 |
| A | HOH2214 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 401 |
| Chain | Residue |
| B | ASP48 |
| B | GLY60 |
| B | ASP62 |
| B | SER64 |
| B | HOH2049 |
| B | HOH2053 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 402 |
| Chain | Residue |
| B | SER170 |
| B | ASP187 |
| B | THR189 |
| B | VAL192 |
| B | ASP194 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | ARG39 |
| B | GLU40 |
| B | PHE46 |
| B | GLU140 |
| B | PRO141 |
| B | LEU166 |
| B | SER168 |
| B | HIS169 |
| B | ALA172 |
| B | ALA173 |
| B | ALA174 |
| B | LEU228 |
| B | SER230 |
| B | MET262 |
| B | HOH2037 |
| B | HOH2039 |
| B | HOH2050 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1330 |
| Chain | Residue |
| A | ARG257 |
| A | HOH2275 |
| B | ASP143 |
| B | SER144 |
| B | SER147 |
| B | HOH2145 |
| B | HOH2152 |
| B | HOH2275 |
| B | HOH2276 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1331 |
| Chain | Residue |
| B | ASP23 |
| B | PHE91 |
| B | LYS94 |
| B | HOH2277 |
| B | HOH2278 |
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":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
