7CK9
Crystal structure of Doxorubicin loaded human ferritin heavy chain
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 | 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 | 0008043 | cellular_component | intracellular ferritin complex |
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 | 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 | 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 | 4 |
Details | binding site for residue CL A 201 |
Chain | Residue |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CL A 202 |
Chain | Residue |
A | GLU162 |
A | GLY164 |
A | HOH372 |
A | HOH571 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CL A 203 |
Chain | Residue |
A | HOH349 |
A | HOH475 |
A | OXY208 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CL A 204 |
Chain | Residue |
A | GLN14 |
A | HOH487 |
A | HOH562 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue MG A 205 |
Chain | Residue |
A | HOH330 |
A | HOH330 |
A | HOH332 |
A | HOH332 |
A | HOH540 |
A | HOH540 |
A | HOH588 |
A | HOH588 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG A 206 |
Chain | Residue |
A | HOH364 |
A | HOH364 |
A | HOH364 |
A | HOH510 |
A | HOH510 |
A | HOH510 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG A 207 |
Chain | Residue |
A | GLU27 |
A | GLU62 |
A | HIS65 |
A | HOH314 |
A | HOH320 |
A | HOH338 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue OXY A 208 |
Chain | Residue |
A | LYS157 |
A | SER163 |
A | GLY164 |
A | LEU165 |
A | CL203 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue GOL A 209 |
Chain | Residue |
A | SER31 |
A | ARG63 |
A | ARG63 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:1992356, ECO:0007744|PDB:1FHA |
Chain | Residue | Details |
A | GLU27 | |
A | HIS65 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085 |
Chain | Residue | Details |
A | GLU62 | |
A | GLU107 | |
A | GLN141 |