1MMM
DISTINCT METAL ENVIRONMENT IN IRON-SUBSTITUTED MANGANESE SUPEROXIDE DISMUTASE PROVIDES A STRUCTURAL BASIS OF METAL SPECIFICITY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0009408 | biological_process | response to heat |
| A | 0010447 | biological_process | response to acidic pH |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071291 | biological_process | cellular response to selenium ion |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0009408 | biological_process | response to heat |
| B | 0010447 | biological_process | response to acidic pH |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071291 | biological_process | cellular response to selenium ion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OH A 207 |
| Chain | Residue |
| A | HIS81 |
| A | GLN146 |
| A | ASP167 |
| A | TRP169 |
| A | HIS171 |
| A | FE206 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OH B 207 |
| Chain | Residue |
| B | TYR34 |
| B | HIS81 |
| B | GLN146 |
| B | ASP167 |
| B | TRP169 |
| B | HIS171 |
| B | FE206 |
| B | OH208 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OH B 208 |
| Chain | Residue |
| B | HIS26 |
| B | HIS30 |
| B | TYR34 |
| B | HIS81 |
| B | HIS171 |
| B | FE206 |
| B | OH207 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 206 |
| Chain | Residue |
| A | HIS26 |
| A | HIS81 |
| A | ASP167 |
| A | HIS171 |
| A | OH207 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 206 |
| Chain | Residue |
| B | HIS26 |
| B | HIS81 |
| B | ASP167 |
| B | HIS171 |
| B | OH207 |
| B | OH208 |
| site_id | FE1 |
| Number of Residues | 6 |
| Details | IRON-SUBSTITUTED ACTIVE SITE CHAIN A. CONTAINS ONE EXOGENOUS LIGAND MODELLED AS HYDROXIDE. |
| Chain | Residue |
| A | FE206 |
| A | HIS26 |
| A | HIS81 |
| A | ASP167 |
| A | HIS171 |
| A | OH207 |
| site_id | FE2 |
| Number of Residues | 7 |
| Details | IRON-SUBSTITUTED ACTIVE SITE CHAIN B. CONTAINS TWO EXOGENOUS LIGANDS BOTH MODELLED AS HYDROXIDES. |
| Chain | Residue |
| B | ASP167 |
| B | HIS171 |
| B | OH207 |
| B | OH208 |
| B | FE206 |
| B | HIS26 |
| B | HIS81 |
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 | ASP167-TYR174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
