2JI3
X-ray structure of the iron-peroxide intermediate of superoxide reductase (E114A mutant) from Desulfoarculus baarsii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050605 | molecular_function | superoxide reductase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050605 | molecular_function | superoxide reductase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009636 | biological_process | response to toxic substance |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019430 | biological_process | removal of superoxide radicals |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050605 | molecular_function | superoxide reductase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009636 | biological_process | response to toxic substance |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050605 | molecular_function | superoxide reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A1127 |
| Chain | Residue |
| A | CYS10 |
| A | CYS13 |
| A | CYS29 |
| A | CYS30 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A1128 |
| Chain | Residue |
| A | NO31131 |
| A | HIS49 |
| A | HIS69 |
| A | HIS75 |
| A | CYS116 |
| A | HIS119 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A1129 |
| Chain | Residue |
| A | ASP33 |
| A | HOH2035 |
| A | HOH2036 |
| C | GLU26 |
| C | HOH2019 |
| C | HOH2029 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A1130 |
| Chain | Residue |
| A | ASP33 |
| A | HOH2026 |
| C | GLU26 |
| C | ASP33 |
| C | HOH2026 |
| C | HOH2027 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 A1131 |
| Chain | Residue |
| A | LYS48 |
| A | HIS49 |
| A | HIS69 |
| A | PRO70 |
| A | HIS75 |
| A | HIS119 |
| A | FE1128 |
| A | HOH2052 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B1127 |
| Chain | Residue |
| B | CYS10 |
| B | CYS13 |
| B | CYS29 |
| B | CYS30 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B1128 |
| Chain | Residue |
| B | HIS49 |
| B | HIS69 |
| B | HIS75 |
| B | CYS116 |
| B | HIS119 |
| B | PER1130 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B1129 |
| Chain | Residue |
| A | HOH2072 |
| B | GLU18 |
| B | THR90 |
| B | HOH2023 |
| B | HOH2024 |
| B | HOH2075 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C1127 |
| Chain | Residue |
| C | CYS10 |
| C | CYS13 |
| C | CYS29 |
| C | CYS30 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C1128 |
| Chain | Residue |
| C | HIS49 |
| C | HIS69 |
| C | HIS75 |
| C | CYS116 |
| C | HIS119 |
| C | PER1130 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CA C1129 |
| Chain | Residue |
| C | GLU18 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D1127 |
| Chain | Residue |
| D | CYS10 |
| D | CYS13 |
| D | CYS29 |
| D | CYS30 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D1128 |
| Chain | Residue |
| D | HIS49 |
| D | HIS69 |
| D | HIS75 |
| D | CYS116 |
| D | HIS119 |
| D | PER1129 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PER B1130 |
| Chain | Residue |
| B | LYS48 |
| B | HIS49 |
| B | HIS69 |
| B | HIS75 |
| B | HIS119 |
| B | FE1128 |
| B | HOH2052 |
| B | HOH2087 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PER C1130 |
| Chain | Residue |
| C | HIS49 |
| C | HIS69 |
| C | HIS75 |
| C | HIS119 |
| C | FE1128 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PER D1129 |
| Chain | Residue |
| D | LYS48 |
| D | HIS49 |
| D | HIS69 |
| D | HIS75 |
| D | HIS119 |
| D | FE1128 |
| D | HOH2058 |
| D | HOH2059 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1do6 |
| Chain | Residue | Details |
| A | LYS48 | |
| A | GLU47 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1do6 |
| Chain | Residue | Details |
| B | LYS48 | |
| B | GLU47 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1do6 |
| Chain | Residue | Details |
| C | LYS48 | |
| C | GLU47 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1do6 |
| Chain | Residue | Details |
| D | LYS48 | |
| D | GLU47 |
