Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0005506 | molecular_function | iron ion binding |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0005776 | cellular_component | autophagosome |
| X | 0006826 | biological_process | iron ion transport |
| X | 0006879 | biological_process | intracellular iron ion homeostasis |
| X | 0008198 | molecular_function | ferrous iron binding |
| X | 0008199 | molecular_function | ferric iron binding |
| X | 0031410 | cellular_component | cytoplasmic vesicle |
| X | 0044754 | cellular_component | autolysosome |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0070288 | cellular_component | ferritin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 X 175 |
| Chain | Residue |
| X | GLN6 |
| X | ASN7 |
| X | HOH249 |
| X | HOH277 |
| X | HOH294 |
| X | HOH373 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 X 176 |
| Chain | Residue |
| X | HOH201 |
| X | HOH338 |
| X | GLN86 |
| X | ASP87 |
| X | GLU88 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PLL X 180 |
| Chain | Residue |
| X | HIS114 |
| X | CYS126 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PLL X 181 |
| Chain | Residue |
| X | SER118 |
| X | CYS126 |
| X | HOH353 |
| X | HOH353 |
| X | HOH353 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PLL X 182 |
| Chain | Residue |
| X | PHE35 |
| X | ASP38 |
| X | CYS48 |
| X | PLL183 |
| X | HOH337 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PLL X 183 |
| Chain | Residue |
| X | CYS48 |
| X | ALA49 |
| X | HIS52 |
| X | PLL182 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PLL X 184 |
| Chain | Residue |
| X | CYS45 |
| X | PLL185 |
| X | EDO187 |
| X | HOH216 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PLL X 185 |
| Chain | Residue |
| X | CYS45 |
| X | HIS173 |
| X | PLL184 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD X 177 |
| Chain | Residue |
| X | ASP80 |
| X | ASP80 |
| X | HOH350 |
| X | HOH350 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO X 178 |
| Chain | Residue |
| X | THR10 |
| X | GLU11 |
| X | ALA14 |
| X | HOH256 |
| X | HOH308 |
| X | HOH387 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO X 179 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO X 186 |
| Chain | Residue |
| X | TYR36 |
| X | GLY90 |
| X | THR91 |
| X | GLU163 |
| X | EDO189 |
| X | HOH193 |
| X | HOH392 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO X 187 |
| Chain | Residue |
| X | LYS143 |
| X | ASP146 |
| X | PLL184 |
| X | HOH231 |
| X | HOH266 |
| X | HOH291 |
| X | HOH335 |
| X | HOH394 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO X 188 |
| Chain | Residue |
| X | HIS52 |
| X | GLU63 |
| X | HOH200 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO X 189 |
| Chain | Residue |
| X | TYR36 |
| X | ARG39 |
| X | ASP41 |
| X | EDO186 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO X 190 |
| Chain | Residue |
| X | ASP80 |
| X | ASP80 |
| X | ASP80 |
| X | GLN82 |
| X | HOH351 |
| X | HOH369 |
| X | HOH395 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO X 191 |
| Chain | Residue |
| X | SER1 |
| X | ARG39 |
| X | GLU88 |
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 |
| X | ASP122-LYS142 | |
| site_id | PS00540 |
| Number of Residues | 19 |
| Details | FERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR |
| Chain | Residue | Details |
| X | GLU57-ARG75 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 149 |
| Details | Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Region: {"description":"Catalytic site for iron oxidation"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"7026284","evidenceCode":"ECO:0000269"}]} |