Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004322 | molecular_function | ferroxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140315 | molecular_function | iron ion sequestering activity |
| B | 0004322 | molecular_function | ferroxidase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006826 | biological_process | iron ion transport |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0140315 | molecular_function | iron ion sequestering activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 200 |
| Chain | Residue |
| A | GLU18 |
| A | GLU51 |
| A | HIS54 |
| A | GLU127 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 201 |
| Chain | Residue |
| A | ARG117 |
| A | ARG155 |
| A | HOH430 |
| B | ARG125 |
| B | ARG128 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 202 |
| Chain | Residue |
| A | ARG39 |
| A | TRP133 |
| A | ARG135 |
| A | HOH362 |
| A | HOH427 |
| A | HOH428 |
| A | HOH441 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 200 |
| Chain | Residue |
| B | GLU18 |
| B | GLU51 |
| B | HIS54 |
| B | GLU127 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 203 |
| Chain | Residue |
| A | LEU19 |
| A | ASN23 |
| A | PHE26 |
| A | TYR45 |
| A | ILE49 |
| A | MET52 |
| A | LYS53 |
| A | HOH330 |
| A | HOH358 |
| A | HOH414 |
| B | ILE22 |
| B | ASN23 |
| B | TYR45 |
| B | ILE49 |
| B | MET52 |
| B | ALA55 |
| B | ASP56 |
| B | ILE59 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A 204 |
| Chain | Residue |
| A | LEU19 |
| A | ILE22 |
| A | ASN23 |
| A | TYR45 |
| A | ILE49 |
| A | MET52 |
| A | ALA55 |
| A | ASP56 |
| A | ILE59 |
| A | HOH330 |
| A | HOH358 |
| A | HOH368 |
| A | HOH414 |
| B | LEU19 |
| B | PHE26 |
| B | TYR45 |
| B | ILE49 |
| B | MET52 |
| B | LYS53 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | LEU14 |
| A | ASN17 |
| A | GLU18 |
| A | TYR58 |
| A | GLY97 |
| A | ILE123 |
| A | GLU127 |
| A | HOH309 |
| A | HOH315 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | GLU47 |
| A | ASP50 |
| A | GLU51 |
| A | HIS54 |
| A | GLU94 |
| A | GLU127 |
| A | HIS130 |
| A | HOH415 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 301 |
| Chain | Residue |
| B | LEU14 |
| B | ASN17 |
| B | GLU18 |
| B | TYR58 |
| B | GLY97 |
| B | LEU101 |
| B | ILE123 |
| B | GLU127 |
| B | HOH329 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | GLU47 |
| B | ASP50 |
| B | GLU51 |
| B | GLU94 |
| B | GLU127 |
| B | HIS130 |
Functional Information from PROSITE/UniProt
| site_id | PS00549 |
| Number of Residues | 19 |
| Details | BACTERIOFERRITIN Bacterioferritin signature. MkGdtkVInyLnklLgneL |
| Chain | Residue | Details |
| A | MET1-LEU19 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 288 |
| Details | Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17077480","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17077480","evidenceCode":"ECO:0000269"}]} |
