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 | 18 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29915379, ECO:0007744|PDB:5OC0 |
Chain | Residue | Details |
A | MSE1-ARG7 | |
A | LYS65-PRO77 |
site_id | SWS_FT_FI2 |
Number of Residues | 92 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:29915379, ECO:0007744|PDB:5OC0 |
Chain | Residue | Details |
A | LEU8-PHE29 | |
A | LEU40-LEU64 | |
A | MSE78-VAL103 | |
A | TRP136-HIS158 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:29915379, ECO:0007744|PDB:5OC0 |
Chain | Residue | Details |
A | ARG30-PRO39 | |
A | MSE104-SER135 |
site_id | SWS_FT_FI4 |
Number of Residues | 17 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:29915379, ECO:0007744|PDB:5OC0 |
Chain | Residue | Details |
A | HIS159-SER176 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:29915379, ECO:0007744|PDB:5OC0 |
Chain | Residue | Details |
A | HIS13 | |
A | HIS45 | |
A | HIS137 | |
A | HIS151 |