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 | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005764 | cellular_component | lysosome |
A | 0005776 | cellular_component | autophagosome |
A | 0005829 | cellular_component | cytosol |
A | 0006826 | biological_process | iron ion transport |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0006880 | biological_process | intracellular sequestering of iron ion |
A | 0006955 | biological_process | immune response |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008199 | molecular_function | ferric iron binding |
A | 0008285 | biological_process | negative regulation of cell population proliferation |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0042802 | molecular_function | identical protein binding |
A | 0044754 | cellular_component | autolysosome |
A | 0046872 | molecular_function | metal ion binding |
A | 0048147 | biological_process | negative regulation of fibroblast proliferation |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070288 | cellular_component | ferritin complex |
A | 0110076 | biological_process | negative regulation of ferroptosis |
A | 0140315 | molecular_function | iron ion sequestering activity |
A | 1904724 | cellular_component | tertiary granule lumen |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue BCN A 201 |
Chain | Residue |
A | SER31 |
A | SER31 |
A | TYR32 |
A | ARG63 |
A | ARG63 |
A | ILE85 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue FE2 A 202 |
Chain | Residue |
A | FE2205 |
A | HOH474 |
A | HOH610 |
A | HOH616 |
A | GLU27 |
A | GLU62 |
A | HIS65 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue FE2 A 203 |
Chain | Residue |
A | HOH332 |
A | HOH332 |
A | HOH332 |
A | HOH403 |
A | HOH403 |
A | HOH403 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue FE2 A 204 |
Chain | Residue |
A | GLN58 |
A | GLU61 |
A | HOH589 |
A | HOH606 |
A | HOH613 |
A | HOH617 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue FE2 A 205 |
Chain | Residue |
A | GLU62 |
A | GLU107 |
A | GLN141 |
A | FE2202 |
A | HOH474 |
A | HOH610 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue FE2 A 206 |
Chain | Residue |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | CL214 |
A | CL214 |
A | CL214 |
A | CL214 |
A | HOH386 |
A | HOH386 |
A | HOH386 |
A | HOH386 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue FE2 A 207 |
Chain | Residue |
A | ASP131 |
A | ASP131 |
A | ASP131 |
A | HOH301 |
A | HOH301 |
A | HOH301 |
A | HOH309 |
A | HOH309 |
A | HOH309 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue FE2 A 208 |
Chain | Residue |
A | HIS57 |
A | GLU61 |
A | HOH544 |
A | HOH592 |
A | HOH595 |
A | HOH619 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue MG A 209 |
Chain | Residue |
A | HOH305 |
A | HOH305 |
A | HOH311 |
A | HOH311 |
A | HOH413 |
A | HOH413 |
A | HOH437 |
A | HOH437 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG A 210 |
Chain | Residue |
A | HOH345 |
A | HOH349 |
A | HOH355 |
A | HOH376 |
A | HOH422 |
A | HOH438 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG A 211 |
Chain | Residue |
A | HOH454 |
A | HOH467 |
A | HOH536 |
A | HOH576 |
A | HOH607 |
A | HOH612 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MG A 212 |
Chain | Residue |
A | HOH466 |
A | HOH516 |
A | HOH517 |
A | HOH525 |
A | HOH583 |
A | HOH618 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue CL A 213 |
Chain | Residue |
A | GLN83 |
A | ASP84 |
A | LYS86 |
A | CL223 |
A | HOH413 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue CL A 214 |
Chain | Residue |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | FE2206 |
A | FE2206 |
A | FE2206 |
A | FE2206 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue CL A 215 |
Chain | Residue |
A | HOH611 |
A | HIS13 |
A | GLN14 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue CL A 216 |
Chain | Residue |
A | GLN75 |
A | ASN139 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue CL A 217 |
Chain | Residue |
A | ASN125 |
A | HOH366 |
A | HOH426 |
site_id | AD9 |
Number of Residues | 1 |
Details | binding site for residue CL A 218 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue CL A 219 |
Chain | Residue |
A | ASP150 |
A | HIS151 |
A | ASN154 |
A | HOH434 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue CL A 220 |
Chain | Residue |
A | ASN25 |
A | HOH527 |
A | HOH570 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue CL A 221 |
Chain | Residue |
A | ARG9 |
A | ASN11 |
A | TYR12 |
A | HOH397 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue CL A 222 |
Chain | Residue |
A | GLN75 |
A | HOH333 |
A | HOH390 |
A | HOH394 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue CL A 223 |
Chain | Residue |
A | LYS86 |
A | CL213 |
A | HOH343 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue CL A 224 |
Chain | Residue |
A | HIS105 |
A | LEU106 |
A | ASN109 |
A | HOH582 |
Functional Information from PROSITE/UniProt
site_id | PS00204 |
Number of Residues | 21 |
Details | FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLneqvkaIK |
Chain | Residue | Details |
A | ASP126-LYS146 | |
site_id | PS00540 |
Number of Residues | 19 |
Details | FERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR |
Chain | Residue | Details |
A | GLU61-ARG79 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU27 | |
A | HIS65 | |
Chain | Residue | Details |
A | GLU62 | |
A | GLU107 | |
A | GLN141 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Essential for association with cargo receptor NCOA4 => ECO:0000269|PubMed:26436293 |
Chain | Residue | Details |
A | ARG22 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | SER178 | |
Chain | Residue | Details |
A | SER182 | |