4DYX
Crystal Structure of the Cu-adduct of Human H-Ferritin variant 4His-delta C-star
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 | 5 |
Details | BINDING SITE FOR RESIDUE CU A 201 |
Chain | Residue |
A | HIS56 |
A | HIS60 |
A | HIS63 |
A | HIS67 |
A | HOH391 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CU A 202 |
Chain | Residue |
A | HOH456 |
A | HOH456 |
A | HOH456 |
A | HOH456 |
A | HOH502 |
A | HOH502 |
A | HOH502 |
A | HOH502 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
A | HIS173 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CU A 203 |
Chain | Residue |
A | GLU27 |
A | GLU62 |
A | HIS65 |
A | CU204 |
A | HOH341 |
A | HOH399 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 204 |
Chain | Residue |
A | GLU62 |
A | GLU107 |
A | CU203 |
A | HOH355 |
A | HOH399 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 205 |
Chain | Residue |
A | ASP84 |
A | ASP84 |
A | GLN86 |
A | GLN86 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CA A 206 |
Chain | Residue |
A | ASP131 |
A | ASP131 |
A | ASP131 |
A | GLU134 |
A | GLU134 |
A | GLU134 |
A | CA207 |
A | CA207 |
A | CA207 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CA A 207 |
Chain | Residue |
A | ASP131 |
A | ASP131 |
A | ASP131 |
A | GLU134 |
A | GLU134 |
A | GLU134 |
A | CA206 |
A | CA206 |
A | CA206 |
A | HOH449 |
A | HOH449 |
A | HOH449 |
Functional Information from PROSITE/UniProt
site_id | PS00204 |
Number of Residues | 21 |
Details | FERRITIN_2 Ferritin iron-binding regions signature 2. DphLADFIEthYLneqvkaIK |
Chain | Residue | Details |
A | ASP126-LYS146 |
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 |