Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004784 | molecular_function | superoxide dismutase activity |
A | 0006801 | biological_process | superoxide metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004784 | molecular_function | superoxide dismutase activity |
B | 0006801 | biological_process | superoxide metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0004784 | molecular_function | superoxide dismutase activity |
C | 0006801 | biological_process | superoxide metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004784 | molecular_function | superoxide dismutase activity |
D | 0006801 | biological_process | superoxide metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 301 |
Chain | Residue |
A | HIS26 |
A | HIS81 |
A | ASP168 |
A | HIS172 |
A | HOH403 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 301 |
Chain | Residue |
B | HOH401 |
B | HIS26 |
B | HIS81 |
B | ASP168 |
B | HIS172 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 301 |
Chain | Residue |
C | HIS26 |
C | HIS81 |
C | ASP168 |
C | HIS172 |
C | HOH402 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRS C 302 |
Chain | Residue |
A | PHE11 |
A | GLY12 |
A | GLY20 |
A | GLN21 |
A | HOH447 |
C | GLN179 |
C | MLY181 |
C | HOH433 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 302 |
Chain | Residue |
D | HIS26 |
D | HIS81 |
D | ASP168 |
D | HIS172 |
D | HOH403 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 303 |
Chain | Residue |
B | GLU15 |
B | GLY20 |
B | GLN21 |
D | TYR178 |
D | MLY181 |
D | ASP184 |
D | HOH520 |
Functional Information from PROSITE/UniProt
site_id | PS00088 |
Number of Residues | 8 |
Details | SOD_MN Manganese and iron superoxide dismutases signature. DaWEHAYY |
Chain | Residue | Details |
A | ASP168-TYR175 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS26 | |
C | HIS81 | |
C | ASP168 | |
C | HIS172 | |
D | HIS26 | |
D | HIS81 | |
D | ASP168 | |
D | HIS172 | |
A | HIS81 | |
A | ASP168 | |
A | HIS172 | |
B | HIS26 | |
B | HIS81 | |
B | ASP168 | |
B | HIS172 | |
C | HIS26 | |
Chain | Residue | Details |
A | THR121 | |
A | THR123 | |
B | THR121 | |
B | THR123 | |
C | THR121 | |
C | THR123 | |
D | THR121 | |
D | THR123 | |