2JI1
X-ray structure of wild-type superoxide reductase 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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A1128 |
| Chain | Residue |
| A | GLU18 |
| A | HOH2042 |
| A | HOH2043 |
| B | HOH2193 |
| B | HOH2196 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A1129 |
| Chain | Residue |
| A | ASP33 |
| A | HOH2074 |
| A | HOH2076 |
| C | GLU26 |
| C | HOH2051 |
| C | HOH2064 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A1130 |
| Chain | Residue |
| A | HIS49 |
| A | HIS69 |
| A | HIS75 |
| A | CYS116 |
| A | HIS119 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B1127 |
| Chain | Residue |
| B | CYS10 |
| B | CYS13 |
| B | CYS29 |
| B | CYS30 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B1128 |
| Chain | Residue |
| B | HIS49 |
| B | HIS69 |
| B | HIS75 |
| B | CYS116 |
| B | HIS119 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C1127 |
| Chain | Residue |
| C | CYS10 |
| C | CYS13 |
| C | CYS29 |
| C | CYS30 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C1128 |
| Chain | Residue |
| A | ASP33 |
| A | HOH2057 |
| C | GLU26 |
| C | ASP33 |
| C | HOH2068 |
| C | HOH2069 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C1129 |
| Chain | Residue |
| C | GLU18 |
| C | HOH2039 |
| C | HOH2136 |
| D | HOH2142 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 C1130 |
| Chain | Residue |
| C | HIS49 |
| C | HIS69 |
| C | HIS75 |
| C | CYS116 |
| C | HIS119 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D1127 |
| Chain | Residue |
| D | CYS10 |
| D | CYS13 |
| D | CYS29 |
| D | CYS30 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 D1128 |
| Chain | Residue |
| D | HIS49 |
| D | HIS69 |
| D | HIS75 |
| D | CYS116 |
| D | HIS119 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS10 | |
| B | CYS10 | |
| B | CYS13 | |
| B | CYS29 | |
| B | CYS30 | |
| B | HIS49 | |
| B | HIS69 | |
| B | HIS75 | |
| B | CYS116 | |
| B | HIS119 | |
| C | CYS10 | |
| A | CYS13 | |
| C | CYS13 | |
| C | CYS29 | |
| C | CYS30 | |
| C | HIS49 | |
| C | HIS69 | |
| C | HIS75 | |
| C | CYS116 | |
| C | HIS119 | |
| D | CYS10 | |
| D | CYS13 | |
| A | CYS29 | |
| D | CYS29 | |
| D | CYS30 | |
| D | HIS49 | |
| D | HIS69 | |
| D | HIS75 | |
| D | CYS116 | |
| D | HIS119 | |
| A | CYS30 | |
| A | HIS49 | |
| A | HIS69 | |
| A | HIS75 | |
| A | CYS116 | |
| A | HIS119 |
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 |
