Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005764 | cellular_component | lysosome |
| A | 0005776 | cellular_component | autophagosome |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0044754 | cellular_component | autolysosome |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070288 | cellular_component | ferritin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD A 185 |
| Chain | Residue |
| A | ASP84 |
| A | ASP84 |
| A | GLN86 |
| A | GLN86 |
| A | HOH410 |
| A | HOH410 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 186 |
| Chain | Residue |
| A | ASP131 |
| A | ASP131 |
| A | ASP131 |
| A | SER135 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 187 |
| Chain | Residue |
| A | ASP42 |
| A | GLU49 |
| A | CYS52 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 188 |
| Chain | Residue |
| A | GLU134 |
| A | GLU134 |
| A | HOH358 |
| A | HOH358 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 189 |
| Chain | Residue |
| A | HIS118 |
| A | CYS130 |
| A | GLU134 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD A 190 |
| Chain | Residue |
| A | HIS136 |
| A | ASP139 |
| site_id | NCL |
| Number of Residues | 4 |
| Details | PUTATIVE IRON CORE NUCLEATION SITE IN FERRITINS. |
| Chain | Residue |
| A | GLU57 |
| A | GLU60 |
| A | GLU61 |
| A | GLU64 |
| site_id | SS1 |
| Number of Residues | 1 |
| Details | INTERMOLECULAR CRYSTAL CONTACT. THIS CADMIUM BRIDGE LINKS 2 SUBUNITS OF NEIGHBORING MOLECULES. |
| site_id | SS2 |
| Number of Residues | 3 |
| Details | THESE CADMIUM ATOMS ARE OBSERVED ON OR NEAR THE CRYSTALLOGRAPHIC THREE-FOLD AXIS. RESIDUE 186 IS LOCATED ON THE AXIS AND THUS HAS AN OCCUPANCY OF 1/3. THE OTHER METAL IONS EXHIBIT DISORDER, WITH THE SITES BEING OCCUPIED ONE THIRD BY METAL AND TWO THIRDS BY WATER MOLECULES. |
| Chain | Residue |
| A | CD186 |
| A | CD188 |
| A | CD189 |
| site_id | SS3 |
| Number of Residues | 1 |
| Details | METAL BINDING SITE ON THE INNER SURFACE OF THE PROTEIN SHELL. THIS MAY NOT BE FUNCTIONALLY SIGNIFICANT SINCE THE LIGANDS OF THIS SITE (ASP 42, GLU 49, AND CYS 52) ARE NOT CONSERVED ACROSS THE FERRITINS. |
Functional Information from PROSITE/UniProt
| site_id | PS00204 |
| Number of Residues | 21 |
| Details | FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEshFLdeevklIK |
| Chain | Residue | Details |
| A | ASP126-LYS146 | |
| site_id | PS00540 |
| Number of Residues | 19 |
| Details | FERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR |
| Chain | Residue | Details |
| A | GLU61-ARG79 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | LEU58 | |
| A | GLU61 | |
| A | LYS62 | |
| A | GLY65 | |
| A | ARG68 | |
