Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000303 | biological_process | response to superoxide |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| B | 0000303 | biological_process | response to superoxide |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046914 | molecular_function | transition metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 193 |
| Chain | Residue |
| A | HIS26 |
| A | HIS73 |
| A | ASP156 |
| A | HIS160 |
| A | HOH196 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 393 |
| Chain | Residue |
| B | HOH394 |
| B | HIS226 |
| B | HIS273 |
| B | ASP356 |
| B | HIS360 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS A 194 |
| Chain | Residue |
| A | SER51 |
| A | GLU54 |
| B | TRS1 |
| B | GLY249 |
| B | HOH429 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS A 195 |
| Chain | Residue |
| A | ASP165 |
| A | HOH230 |
| A | HOH266 |
| A | HOH269 |
| B | GLU260 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS B 1 |
| Chain | Residue |
| A | GLY49 |
| A | TRS194 |
| B | GLY249 |
| B | LYS250 |
| B | SER251 |
| B | GLU254 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS B 4 |
| Chain | Residue |
| A | HOH372 |
| B | GLU221 |
| B | ARG257 |
| B | SER258 |
| B | SER259 |
| B | HOH513 |
| B | HOH560 |
Functional Information from PROSITE/UniProt
| site_id | PS00088 |
| Number of Residues | 8 |
| Details | SOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY |
| Chain | Residue | Details |
| A | ASP156-TYR163 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
