5N26
X-ray structure of human heavy chain ferritin in complex with cisplatin
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 | 3 |
| Details | binding site for residue CPT A 201 |
| Chain | Residue |
| A | LYS68 |
| A | THR135 |
| A | HIS136 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue 73M A 202 |
| Chain | Residue |
| A | CYS102 |
| A | HIS105 |
| A | LYS108 |
| A | ASN109 |
| A | CPT203 |
| A | HOH464 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CPT A 203 |
| Chain | Residue |
| A | ASP89 |
| A | TRP93 |
| A | CYS102 |
| A | 73M202 |
| A | CPT204 |
| A | HOH446 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CPT A 204 |
| Chain | Residue |
| A | CYS90 |
| A | ASP92 |
| A | ASN98 |
| A | CPT203 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 205 |
| Chain | Residue |
| A | HIS173 |
| A | HIS173 |
| A | HIS173 |
| A | HIS173 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 206 |
| Chain | Residue |
| A | ARG9 |
| A | ASN11 |
| A | TYR12 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 207 |
| Chain | Residue |
| A | GLN75 |
| A | ASN139 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 208 |
| Chain | Residue |
| A | HIS13 |
| A | GLN14 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 210 |
| Chain | Residue |
| A | GLN83 |
| A | ASP84 |
| A | LYS86 |
| A | HOH482 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 211 |
| Chain | Residue |
| A | HOH333 |
| A | HOH333 |
| A | HOH333 |
| A | HOH475 |
| A | HOH475 |
| A | HOH475 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 212 |
| Chain | Residue |
| A | HOH318 |
| A | HOH318 |
| A | HOH338 |
| A | HOH338 |
| A | HOH482 |
| A | HOH482 |
| A | HOH523 |
| A | HOH523 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 213 |
| Chain | Residue |
| A | HOH383 |
| A | HOH415 |
| A | HOH423 |
| A | HOH441 |
| A | HOH485 |
| A | HOH514 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 214 |
| Chain | Residue |
| A | GLN58 |
| A | GLU61 |
| A | GLU140 |
| A | HOH305 |
| A | HOH313 |
| A | HOH334 |
| A | HOH386 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 215 |
| Chain | Residue |
| A | GLU27 |
| A | GLU62 |
| A | HIS65 |
| A | HOH315 |
| A | HOH349 |
| A | HOH350 |
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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | THR1 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER178 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008 |
| Chain | Residue | Details |
| A | SER182 |
