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 | 0042802 | molecular_function | identical protein binding |
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 | 0042802 | molecular_function | identical protein binding |
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 | 0042802 | molecular_function | identical protein binding |
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 | 0042802 | molecular_function | identical protein binding |
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: BINDING => ECO:0000250|UniProtKB:P80293 |
Chain | Residue | Details |
A | HIS31 | |
C | HIS79 | |
C | ASP165 | |
C | HIS169 | |
D | HIS31 | |
D | HIS79 | |
D | ASP165 | |
D | HIS169 | |
A | HIS79 | |
A | ASP165 | |
A | HIS169 | |
B | HIS31 | |
B | HIS79 | |
B | ASP165 | |
B | HIS169 | |
C | HIS31 |