3R2S
2.1A resolution structure of Doubly Soaked FtnA from Pseudomonas aeruginosa (pH 6.0)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004322 | molecular_function | ferroxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140315 | molecular_function | iron ion sequestering activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 155 |
| Chain | Residue |
| A | GLU18 |
| A | GLU51 |
| A | HIS54 |
| A | HOH204 |
| A | HOH214 |
| A | HOH224 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 156 |
| Chain | Residue |
| A | FE157 |
| A | HOH204 |
| A | GLU51 |
| A | GLU93 |
| A | HIS130 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 157 |
| Chain | Residue |
| A | GLU47 |
| A | GLU50 |
| A | HIS130 |
| A | FE156 |
| A | FE158 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 158 |
| Chain | Residue |
| A | GLU50 |
| A | ASP129 |
| A | HIS130 |
| A | FE157 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NA A 159 |
| Chain | Residue |
| A | ASN148 |
| A | ASN148 |
| A | ASN148 |
| A | ASN148 |
| A | GLN151 |
| A | GLN151 |
| A | GLN151 |
| A | GLN151 |
| A | HOH223 |
| A | HOH223 |
| A | HOH223 |
| A | HOH223 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 160 |
| Chain | Residue |
| A | ARG116 |
| A | ARG116 |
| A | ARG116 |
| A | LYS120 |
Functional Information from PROSITE/UniProt
| site_id | PS00549 |
| Number of Residues | 19 |
| Details | BACTERIOFERRITIN Bacterioferritin signature. MqGhpeVIdyLntlLtgeL |
| Chain | Residue | Details |
| A | MET1-LEU19 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 144 |
| Details | Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21574546","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R2M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R2S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21574546","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R2M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R2R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21574546","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R2S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Dual function in ferroxidase center and iron gate","evidences":[{"source":"PubMed","id":"21574546","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
