4GU7
Crystal structure of DyP-type peroxidase (SCO7193) from Streptomyces coelicolor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | ASP146 |
| A | ARG207 |
| A | HIS225 |
| A | VAL226 |
| A | THR229 |
| A | SER230 |
| A | ARG243 |
| A | ASN245 |
| A | PHE260 |
| A | MET273 |
| A | ILE289 |
| A | VAL151 |
| A | SER293 |
| A | ASP152 |
| A | GLY153 |
| A | THR154 |
| A | GLU155 |
| A | GLN184 |
| A | TYR186 |
| A | HIS188 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 401 |
| Chain | Residue |
| B | ASP146 |
| B | VAL151 |
| B | ASP152 |
| B | GLY153 |
| B | THR154 |
| B | GLU155 |
| B | GLN184 |
| B | TYR186 |
| B | HIS188 |
| B | ARG207 |
| B | HIS225 |
| B | THR229 |
| B | SER230 |
| B | ARG243 |
| B | ASN245 |
| B | PHE260 |
| B | MET273 |
| B | MET277 |
| B | ILE289 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 401 |
| Chain | Residue |
| C | ASP146 |
| C | PHE150 |
| C | VAL151 |
| C | ASP152 |
| C | GLY153 |
| C | THR154 |
| C | GLU155 |
| C | GLN184 |
| C | TYR186 |
| C | HIS188 |
| C | ARG207 |
| C | HIS225 |
| C | THR229 |
| C | ARG243 |
| C | ASN245 |
| C | THR258 |
| C | PHE260 |
| C | MET273 |
| C | ILE289 |
| C | SER293 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM D 401 |
| Chain | Residue |
| D | ASP146 |
| D | PHE150 |
| D | VAL151 |
| D | GLY153 |
| D | THR154 |
| D | GLU155 |
| D | GLN184 |
| D | TYR186 |
| D | HIS188 |
| D | ARG207 |
| D | HIS225 |
| D | THR229 |
| D | SER230 |
| D | ARG243 |
| D | ASN245 |
| D | THR258 |
| D | PHE260 |
| D | MET273 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI D 402 |
| Chain | Residue |
| B | GLU268 |
| D | HIS286 |
| D | ASP291 |
