Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005764 | cellular_component | lysosome |
A | 0005776 | cellular_component | autophagosome |
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CD A 201 |
Chain | Residue |
A | ASP80 |
A | ASP80 |
A | HOH437 |
A | HOH437 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CD A 202 |
Chain | Residue |
A | GLU11 |
A | HOH405 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CD A 203 |
Chain | Residue |
A | GLU130 |
A | GLU130 |
A | GLU130 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue FE A 204 |
Chain | Residue |
A | GLU57 |
A | GLU60 |
A | OXY209 |
A | PER210 |
A | PER211 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue FE A 205 |
Chain | Residue |
A | GLU56 |
A | GLU60 |
A | FE206 |
A | OXY209 |
A | PER211 |
A | HOH420 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue FE A 206 |
Chain | Residue |
A | GLU53 |
A | GLU56 |
A | GLU57 |
A | FE205 |
A | OXY209 |
A | PER210 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue FE A 207 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue CL A 208 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue OXY A 209 |
Chain | Residue |
A | GLU56 |
A | GLU57 |
A | GLU60 |
A | FE204 |
A | FE205 |
A | FE206 |
A | PER210 |
A | PER211 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue PER A 210 |
Chain | Residue |
A | GLU53 |
A | GLU57 |
A | FE204 |
A | FE206 |
A | OXY209 |
A | PER211 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue PER A 211 |
Chain | Residue |
A | GLU60 |
A | FE204 |
A | FE205 |
A | OXY209 |
A | PER210 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue GOL A 212 |
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
Chain | Residue | Details |
A | GLU53 | |
A | GLU56 | |
A | GLU57 | |
A | GLU60 | |
A | GLU63 | |