6KMN
Crystal Structure of Dye Decolorizing peroxidase from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004325 | molecular_function | ferrochelatase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0033212 | biological_process | iron import into cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004325 | molecular_function | ferrochelatase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0033212 | biological_process | iron import into cell |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004325 | molecular_function | ferrochelatase activity |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0033212 | biological_process | iron import into cell |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004325 | molecular_function | ferrochelatase activity |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0033212 | biological_process | iron import into cell |
| 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 | ASN181 |
| A | LYS278 |
| A | ARG286 |
| A | LEU306 |
| A | PHE308 |
| A | MET322 |
| A | LEU326 |
| A | LEU332 |
| A | OXY402 |
| A | HOH513 |
| A | HOH524 |
| A | PHE185 |
| A | HOH619 |
| A | LYS186 |
| A | GLY188 |
| A | THR189 |
| A | GLY190 |
| A | MET227 |
| A | PHE244 |
| A | HIS273 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue OXY A 402 |
| Chain | Residue |
| A | ASP187 |
| A | ARG286 |
| A | HEM401 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | MET302 |
| C | HOH611 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue HEM B 401 |
| Chain | Residue |
| B | ASN181 |
| B | PHE185 |
| B | LYS186 |
| B | ASP187 |
| B | GLY188 |
| B | THR189 |
| B | GLY190 |
| B | ILE225 |
| B | MET227 |
| B | PHE244 |
| B | HIS273 |
| B | ALA277 |
| B | LYS278 |
| B | ARG286 |
| B | LEU306 |
| B | PHE308 |
| B | PHE319 |
| B | MET322 |
| B | LEU326 |
| B | LEU332 |
| B | OXY402 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue OXY B 402 |
| Chain | Residue |
| B | ASP187 |
| B | ARG286 |
| B | HEM401 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | ILE225 |
| B | SER327 |
| B | ASN333 |
| B | THR336 |
| B | THR338 |
| B | HOH505 |
| B | HOH515 |
| B | HOH526 |
| B | HOH548 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MPD B 404 |
| Chain | Residue |
| B | ALA118 |
| B | MET119 |
| B | PRO120 |
| D | PRO7 |
| D | TYR9 |
| D | LYS352 |
| D | HOH579 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue HEM C 401 |
| Chain | Residue |
| C | ASN181 |
| C | PHE185 |
| C | LYS186 |
| C | GLY188 |
| C | THR189 |
| C | GLY190 |
| C | MET227 |
| C | PHE244 |
| C | ARG246 |
| C | HIS273 |
| C | ALA277 |
| C | LYS278 |
| C | ARG286 |
| C | LEU306 |
| C | PHE308 |
| C | MET322 |
| C | LEU326 |
| C | LEU332 |
| C | OXY402 |
| C | HOH501 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue OXY C 402 |
| Chain | Residue |
| C | ASP187 |
| C | ARG286 |
| C | PHE308 |
| C | HEM401 |
| site_id | AD1 |
| Number of Residues | 18 |
| Details | binding site for residue HEM D 401 |
| Chain | Residue |
| D | HIS273 |
| D | ARG286 |
| D | LEU306 |
| D | PHE308 |
| D | LEU326 |
| D | LEU332 |
| D | OXY402 |
| D | HOH521 |
| D | ASN181 |
| D | PHE185 |
| D | LYS186 |
| D | ASP187 |
| D | GLY188 |
| D | THR189 |
| D | GLY190 |
| D | ILE225 |
| D | MET227 |
| D | PHE244 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue OXY D 402 |
| Chain | Residue |
| D | ASP187 |
| D | ARG286 |
| D | PHE308 |
| D | HEM401 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 403 |
| Chain | Residue |
| D | LYS351 |
| D | LYS352 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 100 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32971035","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36345957","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KMN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7E5Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"32971035","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36345957","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KMM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KMN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7E5Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32971035","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36345957","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KMM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KMN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7E5Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






