2NYB
Crystal structure of E.Coli Iron Superoxide Dismutase Q69E at 1.1 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000303 | biological_process | response to superoxide |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000303 | biological_process | response to superoxide |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000303 | biological_process | response to superoxide |
| C | 0004784 | molecular_function | superoxide dismutase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006801 | biological_process | superoxide metabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019430 | biological_process | removal of superoxide radicals |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000303 | biological_process | response to superoxide |
| D | 0004784 | molecular_function | superoxide dismutase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006801 | biological_process | superoxide metabolic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 193 |
| Chain | Residue |
| A | HIS26 |
| A | HIS73 |
| A | ASP156 |
| A | HIS160 |
| A | O194 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 193 |
| Chain | Residue |
| B | O194 |
| B | HIS26 |
| B | HIS73 |
| B | ASP156 |
| B | HIS160 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 C 193 |
| Chain | Residue |
| C | HIS26 |
| C | HIS73 |
| C | ASP156 |
| C | HIS160 |
| C | O194 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 D 193 |
| Chain | Residue |
| D | HIS26 |
| D | HIS73 |
| D | ASP156 |
| D | HIS160 |
| D | O194 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE O A 194 |
| Chain | Residue |
| A | GLU69 |
| A | HIS73 |
| A | TRP122 |
| A | ASP156 |
| A | TRP158 |
| A | HIS160 |
| A | FE2193 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE O B 194 |
| Chain | Residue |
| B | GLU69 |
| B | HIS73 |
| B | TRP122 |
| B | ASP156 |
| B | TRP158 |
| B | HIS160 |
| B | FE2193 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE O C 194 |
| Chain | Residue |
| C | GLU69 |
| C | HIS73 |
| C | TRP122 |
| C | ASP156 |
| C | TRP158 |
| C | HIS160 |
| C | FE2193 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE O D 194 |
| Chain | Residue |
| D | GLU69 |
| D | HIS73 |
| D | TRP122 |
| D | ASP156 |
| D | TRP158 |
| D | HIS160 |
| D | FE2193 |
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 | ASP156-TYR163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TYR27 | |
| A | THR74 | |
| A | VAL157 | |
| A | ALA161 | |
| B | TYR27 | |
| B | THR74 | |
| B | VAL157 | |
| B | ALA161 | |
| C | TYR27 | |
| C | THR74 | |
| C | VAL157 | |
| C | ALA161 | |
| D | TYR27 | |
| D | THR74 | |
| D | VAL157 | |
| D | ALA161 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | SER51 | |
| B | SER51 | |
| C | SER51 | |
| D | SER51 |
