5OC0
Structure of E. coli superoxide oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue HEM A 201 |
| Chain | Residue |
| A | TYR5 |
| A | ALA155 |
| A | THR166 |
| A | LEU167 |
| A | ARG169 |
| A | MSE170 |
| A | GOL204 |
| A | HOH301 |
| A | HOH303 |
| A | HOH312 |
| A | HIS13 |
| A | TRP14 |
| A | PHE17 |
| A | ARG59 |
| A | ARG63 |
| A | HIS87 |
| A | TYR91 |
| A | HIS151 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue HEM A 202 |
| Chain | Residue |
| A | TYR24 |
| A | MSE27 |
| A | ARG30 |
| A | HIS45 |
| A | VAL46 |
| A | GLY49 |
| A | ILE50 |
| A | LEU97 |
| A | PRO98 |
| A | GLY101 |
| A | LEU102 |
| A | MSE105 |
| A | ARG108 |
| A | LYS134 |
| A | HIS137 |
| A | ALA141 |
| A | ARG173 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | ARG63 |
| A | ARG63 |
| A | LEU64 |
| A | LEU64 |
| A | TYR66 |
| A | TYR66 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 204 |
| Chain | Residue |
| A | HIS87 |
| A | HIS151 |
| A | HEM201 |
| A | HOH301 |
| A | HOH311 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue 37X A 205 |
| Chain | Residue |
| A | ARG7 |
| A | LEU8 |
| A | SER11 |
| A | LEU15 |
| A | PHE32 |
| A | PRO34 |
| A | ASP37 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"29915379","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OC0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29915379","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OC0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"29915379","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OC0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
