Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 1 |
| Number of Residues | 1 |
| Details | METAL-BINDING SITE. SITE 1 IS EXPOSED TO THE EXTERIOR OF THE PROTEIN SHELL. CD 201 IS LOCATED ON THE THREE-FOLD AXES OF THE MOLECULE WHICH ARE PRESUMED TO BE THE IRON ENTRY ROUTE TO THE INTERIOR OF THE PROTEIN. THIS CADMIUM ATOM HAS THEREFORE A MAXIMUM SITE OCCUPATION FACTOR OF 0.33. |
| site_id | 2 |
| Number of Residues | 1 |
| Details | METAL SITE. SITE 2 IS LOCATED NEAR THE INNER SURFACE OF THE PROTEIN SHELL. CD 202 IS LOCATED ON THE THREE-FOLD AXES OF THE MOLECULE WHICH ARE PRESUMED TO BE THE IRON ENTRY ROUTE TO THE INTERIOR OF THE PROTEIN. THIS CADMIUM ATOM HAS THEREFORE A MAXIMUM SITE OCCUPATION FACTOR OF 0.33. |
| site_id | 3 |
| Number of Residues | 1 |
| Details | METAL-BINDING SITE CD 203 IS LOCATED ON A TWO-FOLD AXIS (MAXIMUM SITE OCCUPATION FACTOR OF 0.5). IT BINDS FERRITIN MOLECULES TOGETHER TO BUILD THE CRYSTAL LATTICE. |
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 201 |
| Chain | Residue |
| A | GLU130 |
| A | GLU130 |
| A | GLU130 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 202 |
| Chain | Residue |
| A | ASP127 |
| A | ASP127 |
| A | ASP127 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 203 |
| Chain | Residue |
| A | ASP80 |
| A | ASP80 |
| A | GLN82 |
| A | GLN82 |
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 | ASP122-LYS142 | |
| site_id | PS00540 |
| Number of Residues | 19 |
| Details | FERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR |
| Chain | Residue | Details |
| A | 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"}]} |
