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 |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005776 | cellular_component | autophagosome |
| B | 0006826 | biological_process | iron ion transport |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0044754 | cellular_component | autolysosome |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070288 | cellular_component | ferritin complex |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005776 | cellular_component | autophagosome |
| C | 0006826 | biological_process | iron ion transport |
| C | 0006879 | biological_process | intracellular iron ion homeostasis |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0008199 | molecular_function | ferric iron binding |
| C | 0031410 | cellular_component | cytoplasmic vesicle |
| C | 0044754 | cellular_component | autolysosome |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070288 | cellular_component | ferritin complex |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005776 | cellular_component | autophagosome |
| D | 0006826 | biological_process | iron ion transport |
| D | 0006879 | biological_process | intracellular iron ion homeostasis |
| D | 0008198 | molecular_function | ferrous iron binding |
| D | 0008199 | molecular_function | ferric iron binding |
| D | 0031410 | cellular_component | cytoplasmic vesicle |
| D | 0044754 | cellular_component | autolysosome |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070288 | cellular_component | ferritin complex |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005776 | cellular_component | autophagosome |
| E | 0006826 | biological_process | iron ion transport |
| E | 0006879 | biological_process | intracellular iron ion homeostasis |
| E | 0008198 | molecular_function | ferrous iron binding |
| E | 0008199 | molecular_function | ferric iron binding |
| E | 0031410 | cellular_component | cytoplasmic vesicle |
| E | 0044754 | cellular_component | autolysosome |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0070288 | cellular_component | ferritin complex |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005776 | cellular_component | autophagosome |
| F | 0006826 | biological_process | iron ion transport |
| F | 0006879 | biological_process | intracellular iron ion homeostasis |
| F | 0008198 | molecular_function | ferrous iron binding |
| F | 0008199 | molecular_function | ferric iron binding |
| F | 0031410 | cellular_component | cytoplasmic vesicle |
| F | 0044754 | cellular_component | autolysosome |
| F | 0046872 | molecular_function | metal ion binding |
| F | 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 3-FOLD AXES OF THE MOLECULE WHICH ARE PRESUMED TO BE THE IRON ENTRY ROUTE TO THE INTERIOR OF THE PROTEIN. THIS CADMIUM ATOM HAS BEEN ASSIGNED LOW SITE OCCUPATION FACTOR, AS COMPARED TO THOSE FOUND IN THE NATIVE CUBIC STRUCTURE (ENTRY CODE 1IER) BUT CLEARLY CANNOT BE CONFUSED WITH SOLVENT MOLECULE. |
| site_id | 1' |
| Number of Residues | 1 |
| Details | METAL-BINDING SITE. SITE 1' IS EXPOSED T THE EXTERIOR OF THE PROTEIN SHELL. CD 203 IS LOCATED ON THE 3-FOLD AXES OF THE MOLECULE WHICH ARE PRESUMED TO BE THE IRON ENTRY ROUTE TO THE INTERIOR OF THE PROTEIN. THIS CADMIUM ATOM HAS BEEN ASSIGNED LOW SITE OCCUPATION FACTOR, AS COMPARED TO THOSE FOUND IN THE NATIVE CUBIC STRUCTURE (ENTRY CODE 1IER) BUT CLEARLY CANNOT BE CONFUSED WITH SOLVENT MOLECULE. |
| 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 3-FOLD AXES OF THE MOLECULE WHICH ARE PRESUMED TO BE THE IRON ENTRY ROUTE TO THE INTERIOR OF THE PROTEIN. THIS CADMIUM ATOM HAS BEEN ASSIGNED LOW SITE OCCUPATION FACTOR, AS COMPARED TO THOSE FOUND IN THE NATIVE CUBIC STRUCTURE (ENTRY CODE 1IER) BUT CLEARLY CANNOT BE CONFUSED WITH SOLVENT MOLECULE. |
| site_id | 2' |
| Number of Residues | 1 |
| Details | METAL SITE. SITE 2' IS LOCATED NEAR THE INNER SURFACE OF THE PROTEIN SHELL. CD 204 IS LOCATED ON THE 3-FOLD AXES OF THE MOLECULE WHICH ARE PRESUMED TO BE THE IRON ENTRY ROUTE TO THE INTERIOR OF THE PROTEIN. THIS CADMIUM ATOM HAS BEEN ASSIGNED LOW SITE OCCUPATION FACTOR, AS COMPARED TO THOSE FOUND IN THE NATIVE CUBIC STRUCTURE (ENTRY CODE 1IER) BUT CLEARLY CANNOT BE CONFUSED WITH SOLVENT MOLECULE. |
| site_id | 3 |
| Number of Residues | 1 |
| Details | METAL-BINDING SITE CD 205 IS LOCATED OUTSIDE OF THE MOLECULE; IT BINDS NEIGHBORING MOLECULES TOGETHER (SEE REFERENCE 1) AND THUS PARTICIPATES TO THE CRYSTAL LATTICE PACKING. |
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 201 |
| Chain | Residue |
| A | GLU130 |
| B | GLU130 |
| C | GLU130 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD B 202 |
| Chain | Residue |
| C | ASP127 |
| B | ASP127 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD D 203 |
| Chain | Residue |
| D | GLU130 |
| E | GLU130 |
| F | GLU130 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 205 |
| Chain | Residue |
| B | THR10 |
| B | GLU11 |
| C | GLU11 |
| C | GLN120 |
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 | 894 |
| Details | Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Region: {"description":"Catalytic site for iron oxidation"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"7026284","evidenceCode":"ECO:0000269"}]} |
