4E6K
2.0 A resolution structure of Pseudomonas aeruginosa bacterioferritin (BfrB) in complex with bacterioferritin associated ferredoxin (Bfd)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004322 | molecular_function | ferroxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0006880 | biological_process | intracellular sequestering of iron ion |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004322 | molecular_function | ferroxidase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006826 | biological_process | iron ion transport |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0006880 | biological_process | intracellular sequestering of iron ion |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004322 | molecular_function | ferroxidase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006826 | biological_process | iron ion transport |
| C | 0006879 | biological_process | intracellular iron ion homeostasis |
| C | 0006880 | biological_process | intracellular sequestering of iron ion |
| C | 0008199 | molecular_function | ferric iron binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004322 | molecular_function | ferroxidase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006826 | biological_process | iron ion transport |
| D | 0006879 | biological_process | intracellular iron ion homeostasis |
| D | 0006880 | biological_process | intracellular sequestering of iron ion |
| D | 0008199 | molecular_function | ferric iron binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004322 | molecular_function | ferroxidase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0006826 | biological_process | iron ion transport |
| E | 0006879 | biological_process | intracellular iron ion homeostasis |
| E | 0006880 | biological_process | intracellular sequestering of iron ion |
| E | 0008199 | molecular_function | ferric iron binding |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004322 | molecular_function | ferroxidase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0006826 | biological_process | iron ion transport |
| F | 0006879 | biological_process | intracellular iron ion homeostasis |
| F | 0006880 | biological_process | intracellular sequestering of iron ion |
| F | 0008199 | molecular_function | ferric iron binding |
| F | 0020037 | molecular_function | heme binding |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051536 | molecular_function | iron-sulfur cluster binding |
| G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051536 | molecular_function | iron-sulfur cluster binding |
| H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051536 | molecular_function | iron-sulfur cluster binding |
| I | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE K A 201 |
| Chain | Residue |
| A | ASN148 |
| A | ASN148 |
| A | ASN148 |
| A | ASN148 |
| A | GLN151 |
| A | GLN151 |
| A | GLN151 |
| A | GLN151 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 202 |
| Chain | Residue |
| A | ILE22 |
| A | ASN23 |
| A | PHE26 |
| A | TYR45 |
| A | ILE49 |
| A | MET52 |
| A | LYS53 |
| A | ILE59 |
| A | LEU71 |
| A | HOH308 |
| A | HOH363 |
| A | HOH387 |
| A | HOH471 |
| A | HOH472 |
| B | LEU19 |
| B | ILE22 |
| B | ASN23 |
| B | PHE26 |
| B | TYR45 |
| B | ILE49 |
| B | MET52 |
| B | LYS53 |
| B | ILE59 |
| A | LEU19 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 203 |
| Chain | Residue |
| A | ASP34 |
| A | ASP132 |
| A | THR136 |
| A | HOH464 |
| A | HOH465 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE K B 201 |
| Chain | Residue |
| B | ASN148 |
| B | GLN151 |
| C | ASN148 |
| C | GLN151 |
| D | ASN148 |
| D | GLN151 |
| E | ASN148 |
| E | GLN151 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 202 |
| Chain | Residue |
| B | ASP132 |
| B | THR136 |
| B | HOH307 |
| C | ASP34 |
| C | HOH441 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM C 201 |
| Chain | Residue |
| C | LEU19 |
| C | ILE22 |
| C | ASN23 |
| C | PHE26 |
| C | TYR45 |
| C | ILE49 |
| C | MET52 |
| C | LYS53 |
| C | ALA55 |
| C | ILE59 |
| C | HOH318 |
| C | HOH352 |
| C | HOH359 |
| C | HOH368 |
| D | LEU19 |
| D | ILE22 |
| D | ASN23 |
| D | PHE26 |
| D | TYR45 |
| D | ILE49 |
| D | MET52 |
| D | LYS53 |
| D | ALA55 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 202 |
| Chain | Residue |
| C | ASP132 |
| C | THR136 |
| C | HOH304 |
| E | ASP34 |
| E | HOH446 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 201 |
| Chain | Residue |
| B | ASP34 |
| D | ASP132 |
| D | THR136 |
| D | HOH427 |
| D | HOH428 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM E 201 |
| Chain | Residue |
| F | PHE26 |
| F | TYR45 |
| F | ILE49 |
| F | MET52 |
| F | LYS53 |
| F | LEU71 |
| E | LEU19 |
| E | ASN23 |
| E | PHE26 |
| E | TYR45 |
| E | ILE49 |
| E | MET52 |
| E | LYS53 |
| E | LEU71 |
| E | HOH342 |
| E | HOH366 |
| E | HOH368 |
| E | HOH389 |
| E | HOH395 |
| F | LEU19 |
| F | ILE22 |
| F | ASN23 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 202 |
| Chain | Residue |
| D | ASP34 |
| E | ASP132 |
| E | THR136 |
| E | HOH302 |
| E | HOH447 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE K F 201 |
| Chain | Residue |
| F | ASN148 |
| F | ASN148 |
| F | ASN148 |
| F | ASN148 |
| F | GLN151 |
| F | GLN151 |
| F | GLN151 |
| F | GLN151 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA F 202 |
| Chain | Residue |
| F | ASP34 |
| F | ASP132 |
| F | THR136 |
| F | HOH465 |
| F | HOH467 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES G 101 |
| Chain | Residue |
| G | CYS4 |
| G | LEU5 |
| G | CYS6 |
| G | GLY35 |
| G | GLN37 |
| G | CYS38 |
| G | GLY39 |
| G | CYS41 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 G 102 |
| Chain | Residue |
| B | LYS76 |
| B | HOH321 |
| G | ARG26 |
| G | ARG29 |
| G | LYS46 |
| G | HOH217 |
| G | HOH226 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES H 101 |
| Chain | Residue |
| H | CYS4 |
| H | LEU5 |
| H | CYS6 |
| H | GLY35 |
| H | GLN37 |
| H | CYS38 |
| H | GLY39 |
| H | CYS41 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES I 101 |
| Chain | Residue |
| I | CYS4 |
| I | LEU5 |
| I | CYS6 |
| I | GLY35 |
| I | GLN37 |
| I | CYS38 |
| I | GLY39 |
| I | CYS41 |
Functional Information from PROSITE/UniProt
| site_id | PS00549 |
| Number of Residues | 19 |
| Details | BACTERIOFERRITIN Bacterioferritin signature. MkGdkkVIqhLnkiLgneL |
| Chain | Residue | Details |
| A | MET1-LEU19 |
