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: |
Chain | Residue | Details |
A | HIS27 | |
A | SER82 | |
A | VAL168 | |
A | ALA172 | |
B | HIS27 | |
B | SER82 | |
B | VAL168 | |
B | ALA172 |