Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 300 |
| Chain | Residue |
| A | HIS48 |
| A | HIS48 |
| A | HIS50 |
| A | HIS50 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 500 |
| Chain | Residue |
| B | HIS48 |
| B | HIS50 |
| B | HIS114 |
| B | HOH1353 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | HIS85 |
| A | HIS94 |
| A | HIS103 |
| A | ASP106 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 402 |
| Chain | Residue |
| A | HIS60 |
| A | HIS62 |
| A | HIS85 |
| A | HIS141 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 600 |
| Chain | Residue |
| B | HIS85 |
| B | HIS94 |
| B | HIS103 |
| B | ASP106 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 602 |
| Chain | Residue |
| B | HIS60 |
| B | HIS62 |
| B | HIS85 |
| B | HIS141 |
| site_id | ACT |
| Number of Residues | 12 |
| Details | COPPER AND ZINC ARE LIGATED BY THREE CONSERVED HISTIDINES EACH IN THE ACTIVE SITE OF EACH SUBUNIT. |
| Chain | Residue |
| A | HIS60 |
| B | HIS94 |
| B | HIS103 |
| B | HIS141 |
| A | HIS62 |
| A | HIS85 |
| A | HIS94 |
| A | HIS103 |
| A | HIS141 |
| B | HIS60 |
| B | HIS62 |
| B | HIS85 |
Functional Information from PROSITE/UniProt
| site_id | PS00087 |
| Number of Residues | 11 |
| Details | SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHQnPScE |
| Chain | Residue | Details |
| A | GLY58-GLU68 | |
| site_id | PS00332 |
| Number of Residues | 12 |
| Details | SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GGGGpRmACgvI |
| Chain | Residue | Details |
| A | GLY155-ILE166 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS67 | |
| B | HIS85 | |
| B | HIS94 | |
| B | HIS103 | |
| B | ASP106 | |
| B | HIS141 | |
| A | PRO69 | |
| A | LYS92 | |
| A | ASN101 | |
| A | LEU110 | |
| A | GLU113 | |
| A | SER148 | |
| B | HIS60 | |
| B | HIS62 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| A | HIS85 | |
| A | ARG160 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| B | HIS85 | |
| B | ARG160 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| A | HIS85 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2jcw |
| Chain | Residue | Details |
| B | HIS85 | |
