3O72
Crystal structure of EfeB in complex with heme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004325 | molecular_function | ferrochelatase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0042597 | cellular_component | periplasmic space |
| 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 | 0005829 | cellular_component | cytosol |
| 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 | 0042597 | cellular_component | periplasmic space |
| 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 | 0005829 | cellular_component | cytosol |
| 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 | 0042597 | cellular_component | periplasmic space |
| 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 | 0005829 | cellular_component | cytosol |
| 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 | 0042597 | cellular_component | periplasmic space |
| 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 | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | HOH11 |
| A | HIS329 |
| A | ALA333 |
| A | ASN334 |
| A | ARG336 |
| A | ARG347 |
| A | PHE368 |
| A | PHE379 |
| A | VAL382 |
| A | GLN383 |
| A | LEU386 |
| A | LEU231 |
| A | HOH436 |
| A | HOH592 |
| A | OXY600 |
| A | LYS234 |
| A | ASP235 |
| A | GLY236 |
| A | THR237 |
| A | ALA238 |
| A | ILE275 |
| A | PHE294 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OXY A 600 |
| Chain | Residue |
| A | ASP235 |
| A | ARG347 |
| A | HEM500 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | HOH4 |
| B | ASN229 |
| B | PHE233 |
| B | LYS234 |
| B | ASP235 |
| B | GLY236 |
| B | THR237 |
| B | ALA238 |
| B | ILE275 |
| B | PHE294 |
| B | HIS329 |
| B | ALA333 |
| B | ASN334 |
| B | ARG336 |
| B | ARG347 |
| B | PHE368 |
| B | PHE379 |
| B | VAL382 |
| B | GLN383 |
| B | LEU386 |
| B | HOH435 |
| B | HOH468 |
| B | HOH501 |
| B | OXY600 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OXY B 600 |
| Chain | Residue |
| B | ASP235 |
| B | ARG347 |
| B | HEM500 |
| B | HOH540 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM C 500 |
| Chain | Residue |
| C | LYS234 |
| C | ASP235 |
| C | GLY236 |
| C | THR237 |
| C | ALA238 |
| C | ILE275 |
| C | PHE277 |
| C | PHE294 |
| C | HIS329 |
| C | ASN334 |
| C | ARG336 |
| C | ARG347 |
| C | LEU366 |
| C | PHE368 |
| C | PHE379 |
| C | GLN383 |
| C | LEU386 |
| C | HOH438 |
| C | OXY600 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OXY C 600 |
| Chain | Residue |
| C | ASP235 |
| C | ARG347 |
| C | HEM500 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM D 500 |
| Chain | Residue |
| D | PHE233 |
| D | LYS234 |
| D | ASP235 |
| D | GLY236 |
| D | THR237 |
| D | ALA238 |
| D | PHE294 |
| D | HIS329 |
| D | ILE330 |
| D | ALA333 |
| D | ASN334 |
| D | ARG336 |
| D | ARG347 |
| D | PHE368 |
| D | PHE379 |
| D | VAL382 |
| D | GLN383 |
| D | LEU386 |
| D | HOH446 |
| D | HOH452 |
| D | HOH536 |
| D | OXY600 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OXY D 600 |
| Chain | Residue |
| D | LEU366 |
| D | HEM500 |
| D | HOH943 |
| D | ASP235 |
| D | ARG347 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21324904","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"21324904","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
