3AK3
Superoxide dismutase from Aeropyrum pernix K1, Fe-bound form
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 |
| C | 0004784 | molecular_function | superoxide dismutase activity |
| C | 0006801 | biological_process | superoxide metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019430 | biological_process | removal of superoxide radicals |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004784 | molecular_function | superoxide dismutase activity |
| D | 0006801 | biological_process | superoxide metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 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 215 |
| Chain | Residue |
| A | HIS31 |
| A | HIS79 |
| A | ASP165 |
| A | HIS169 |
| A | HOH217 |
| A | HOH288 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 216 |
| Chain | Residue |
| C | GLU148 |
| C | VAL152 |
| A | GLU148 |
| A | LYS149 |
| A | HOH394 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 215 |
| Chain | Residue |
| B | HIS31 |
| B | HIS79 |
| B | ASP165 |
| B | HIS169 |
| B | HOH221 |
| B | HOH250 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 216 |
| Chain | Residue |
| B | PRO21 |
| B | ASN185 |
| B | HOH305 |
| B | HOH424 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 217 |
| Chain | Residue |
| B | LYS49 |
| B | ILE60 |
| B | ASP61 |
| B | VAL65 |
| B | HOH297 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 218 |
| Chain | Residue |
| A | LEU153 |
| B | ARG67 |
| B | LYS149 |
| B | ASN151 |
| B | HOH306 |
| C | ARG67 |
| C | HOH266 |
| D | GLU126 |
| D | HOH223 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 219 |
| Chain | Residue |
| A | PRO89 |
| A | GLY90 |
| B | GLU20 |
| B | GLU25 |
| B | HOH233 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 220 |
| Chain | Residue |
| B | ALA64 |
| B | ARG67 |
| B | ASP68 |
| B | HOH243 |
| B | HOH291 |
| C | ALA64 |
| C | ARG67 |
| C | ASP68 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 215 |
| Chain | Residue |
| C | HIS31 |
| C | HIS79 |
| C | ASP165 |
| C | HIS169 |
| C | HOH219 |
| C | HOH253 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 216 |
| Chain | Residue |
| C | LEU142 |
| C | ARG143 |
| C | HOH281 |
| D | LEU47 |
| D | ILE50 |
| D | GLU51 |
| D | HOH269 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 215 |
| Chain | Residue |
| D | HIS31 |
| D | HIS79 |
| D | ASP165 |
| D | HIS169 |
| D | HOH219 |
| D | HOH267 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 216 |
| Chain | Residue |
| A | ARG67 |
| B | HOH225 |
| B | HOH251 |
| C | GLU148 |
| C | LEU153 |
| D | ARG67 |
| D | LYS149 |
| D | HOH261 |
| D | HOH284 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 217 |
| Chain | Residue |
| B | ASN177 |
| D | LYS34 |
| D | HIS35 |
| D | THR38 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 218 |
| Chain | Residue |
| C | ARG63 |
| D | LYS123 |
| D | VAL125 |
| D | GLU126 |
| D | HOH268 |
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 | ASP165-TYR172 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P80293","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






