2JI2
X-ray structure of E114A mutant of superoxide reductase from Desulfoarculus baarsii in the native, reduced form
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 A1000 |
Chain | Residue |
A | CYS10 |
A | CYS13 |
A | CYS29 |
A | CYS30 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 A1127 |
Chain | Residue |
A | HIS119 |
A | FE22000 |
A | HOH2147 |
A | LYS48 |
A | HIS49 |
A | HIS69 |
A | PRO70 |
A | HIS75 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 A2000 |
Chain | Residue |
A | HIS49 |
A | HIS69 |
A | HIS75 |
A | CYS116 |
A | HIS119 |
A | NO31127 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE B1001 |
Chain | Residue |
B | CYS10 |
B | CYS13 |
B | CYS29 |
B | CYS30 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 B1127 |
Chain | Residue |
B | LYS48 |
B | HIS49 |
B | HIS69 |
B | HIS75 |
B | HIS119 |
B | FE21129 |
B | HOH2173 |
B | HOH2174 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B1128 |
Chain | Residue |
A | GLU18 |
A | HOH2026 |
B | GLU18 |
B | HOH2138 |
B | HOH2141 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 B1129 |
Chain | Residue |
B | HIS49 |
B | HIS69 |
B | HIS75 |
B | CYS116 |
B | HIS119 |
B | NO31127 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE C1002 |
Chain | Residue |
C | CYS10 |
C | CYS13 |
C | CYS29 |
C | CYS30 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 C1127 |
Chain | Residue |
C | LYS48 |
C | HIS49 |
C | HIS69 |
C | PRO70 |
C | HIS75 |
C | HIS119 |
C | FE21131 |
C | HOH2127 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C1128 |
Chain | Residue |
C | GLU18 |
C | HOH2029 |
C | HOH2104 |
C | HOH2107 |
D | HOH2030 |
D | HOH2097 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C1129 |
Chain | Residue |
A | ASP33 |
A | HOH2036 |
C | GLU26 |
C | ASP33 |
C | HOH2055 |
C | HOH2056 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C1130 |
Chain | Residue |
A | ASP33 |
A | HOH2050 |
C | GLU26 |
C | HOH2037 |
C | HOH2038 |
C | HOH2041 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 C1131 |
Chain | Residue |
C | HIS49 |
C | HIS69 |
C | HIS75 |
C | CYS116 |
C | HIS119 |
C | NO31127 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE D1003 |
Chain | Residue |
D | CYS10 |
D | CYS13 |
D | CYS29 |
D | CYS30 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 D1127 |
Chain | Residue |
D | LYS48 |
D | HIS49 |
D | HIS69 |
D | PRO70 |
D | HIS75 |
D | HIS119 |
D | FE21128 |
D | HOH2120 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 D1128 |
Chain | Residue |
D | HIS49 |
D | HIS69 |
D | HIS75 |
D | CYS116 |
D | HIS119 |
D | NO31127 |
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 |