Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 202 |
| Chain | Residue |
| A | HIS27 |
| A | HIS75 |
| A | ASP161 |
| A | HIS165 |
| A | F203 |
| A | HOH204 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE F A 203 |
| Chain | Residue |
| A | HIS27 |
| A | TYR35 |
| A | HIS75 |
| A | ASP161 |
| A | HIS165 |
| A | FE202 |
| A | HOH204 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 202 |
| Chain | Residue |
| B | HIS27 |
| B | HIS75 |
| B | ASP161 |
| B | HIS165 |
| B | F203 |
| B | HOH204 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE F B 203 |
| Chain | Residue |
| B | HIS27 |
| B | TYR35 |
| B | HIS75 |
| B | ASP161 |
| B | HIS165 |
| B | FE202 |
| B | HOH204 |
| site_id | FEA |
| Number of Residues | 7 |
| Details | FERRIC IRON (FE(III)), SIX FOLD COORDINATED FLUORIDE AT THE POSSIBLE SUBSTRATE BINDING SITE ACTIVITY COMPETITIVELY HAMPERED |
| Chain | Residue |
| A | FE202 |
| A | HIS27 |
| A | HIS75 |
| A | ASP161 |
| A | HIS165 |
| A | F203 |
| A | HOH204 |
| site_id | FEB |
| Number of Residues | 7 |
| Details | FERRIC IRON (FE(III)), SIX FOLD COORDINATED FLUORIDE AT THE POSSIBLE SUBSTRATE BINDING SITE ACTIVITY COMPETITIVELY HAMPERED |
| Chain | Residue |
| B | HIS75 |
| B | ASP161 |
| B | HIS165 |
| B | F203 |
| B | HOH204 |
| B | FE202 |
| B | HIS27 |
Functional Information from PROSITE/UniProt
| site_id | PS00088 |
| Number of Residues | 8 |
| Details | SOD_MN Manganese and iron superoxide dismutases signature. DmWEHAFY |
| Chain | Residue | Details |
| A | ASP161-TYR168 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS27 | |
| A | HIS75 | |
| A | ASP161 | |
| A | HIS165 | |
| B | HIS27 | |
| B | HIS75 | |
| B | ASP161 | |
| B | HIS165 | |
