1QGH
THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006879 | biological_process | intracellular iron ion homeostasis |
| C | 0008199 | molecular_function | ferric iron binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006879 | biological_process | intracellular iron ion homeostasis |
| D | 0008199 | molecular_function | ferric iron binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006879 | biological_process | intracellular iron ion homeostasis |
| E | 0008199 | molecular_function | ferric iron binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006879 | biological_process | intracellular iron ion homeostasis |
| F | 0008199 | molecular_function | ferric iron binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006879 | biological_process | intracellular iron ion homeostasis |
| G | 0008199 | molecular_function | ferric iron binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006879 | biological_process | intracellular iron ion homeostasis |
| H | 0008199 | molecular_function | ferric iron binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006879 | biological_process | intracellular iron ion homeostasis |
| I | 0008199 | molecular_function | ferric iron binding |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0006879 | biological_process | intracellular iron ion homeostasis |
| J | 0008199 | molecular_function | ferric iron binding |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0006879 | biological_process | intracellular iron ion homeostasis |
| K | 0008199 | molecular_function | ferric iron binding |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0006879 | biological_process | intracellular iron ion homeostasis |
| L | 0008199 | molecular_function | ferric iron binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| L | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 157 |
| Chain | Residue |
| E | HIS31 |
| E | HOH197 |
| G | ASP58 |
| G | GLU62 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE B 157 |
| Chain | Residue |
| E | ASP58 |
| E | GLU62 |
| G | HIS31 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 157 |
| Chain | Residue |
| A | ASP58 |
| A | GLU62 |
| C | HIS31 |
| C | ASP47 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D 157 |
| Chain | Residue |
| A | HIS31 |
| A | ASP47 |
| C | ASP58 |
| C | GLU62 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE E 157 |
| Chain | Residue |
| I | ASP58 |
| I | GLU62 |
| K | HIS31 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE F 157 |
| Chain | Residue |
| F | HIS31 |
| H | ASP58 |
| H | GLU62 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE G 157 |
| Chain | Residue |
| J | ASP58 |
| J | GLU62 |
| J | HOH161 |
| L | HIS31 |
| L | ASP47 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE H 157 |
| Chain | Residue |
| J | HIS31 |
| L | ASP58 |
| L | GLU62 |
| L | HOH158 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE I 157 |
| Chain | Residue |
| I | HIS31 |
| K | ASP58 |
| K | GLU62 |
| site_id | ASA |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| A | GLU62 |
| A | ASP58 |
| A | HIS31 |
| A | ASP47 |
| A | HIS43 |
| site_id | ASB |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| B | HIS43 |
| B | GLU62 |
| B | ASP58 |
| B | HIS31 |
| B | ASP47 |
| site_id | ASC |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| C | GLU62 |
| C | ASP58 |
| C | HIS31 |
| C | ASP47 |
| C | HIS43 |
| site_id | ASD |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| D | GLU62 |
| D | ASP58 |
| D | HIS31 |
| D | ASP47 |
| D | HIS43 |
| site_id | ASE |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| E | GLU62 |
| E | ASP58 |
| E | HIS31 |
| E | ASP47 |
| E | HIS43 |
| site_id | ASF |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| F | GLU62 |
| F | ASP58 |
| F | HIS31 |
| F | ASP47 |
| F | HIS43 |
| site_id | ASG |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| G | GLU62 |
| G | ASP58 |
| G | HIS31 |
| G | ASP47 |
| G | HIS43 |
| site_id | ASH |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| H | GLU62 |
| H | ASP58 |
| H | HIS31 |
| H | ASP47 |
| H | HIS43 |
| site_id | ASI |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| I | GLU62 |
| I | ASP58 |
| I | HIS31 |
| I | ASP47 |
| I | HIS43 |
| site_id | ASJ |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| J | GLU62 |
| J | ASP58 |
| J | HIS31 |
| J | ASP47 |
| J | HIS43 |
| site_id | ASK |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| K | GLU62 |
| K | ASP58 |
| K | HIS31 |
| K | ASP47 |
| K | HIS43 |
| site_id | ASL |
| Number of Residues | 5 |
| Details | IRON-BINDING SITE |
| Chain | Residue |
| L | GLU62 |
| L | ASP58 |
| L | HIS31 |
| L | ASP47 |
| L | HIS43 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE J 157 |
| Chain | Residue |
| B | ASP58 |
| B | GLU62 |
| D | HIS31 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE K 157 |
| Chain | Residue |
| F | ASP58 |
| F | GLU62 |
| H | HIS31 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE L 157 |
| Chain | Residue |
| B | HIS31 |
| D | ASP58 |
| D | GLU62 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10625425 |
| Chain | Residue | Details |
| A | HIS31 | |
| J | HIS31 | |
| K | HIS31 | |
| L | HIS31 | |
| B | HIS31 | |
| C | HIS31 | |
| D | HIS31 | |
| E | HIS31 | |
| F | HIS31 | |
| G | HIS31 | |
| H | HIS31 | |
| I | HIS31 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:10625425 |
| Chain | Residue | Details |
| A | ASP58 | |
| J | ASP58 | |
| K | ASP58 | |
| L | ASP58 | |
| B | ASP58 | |
| C | ASP58 | |
| D | ASP58 | |
| E | ASP58 | |
| F | ASP58 | |
| G | ASP58 | |
| H | ASP58 | |
| I | ASP58 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10625425 |
| Chain | Residue | Details |
| A | GLU62 | |
| J | GLU62 | |
| K | GLU62 | |
| L | GLU62 | |
| B | GLU62 | |
| C | GLU62 | |
| D | GLU62 | |
| E | GLU62 | |
| F | GLU62 | |
| G | GLU62 | |
| H | GLU62 | |
| I | GLU62 |
