3F8D
Structure of Sulfolobus solfataricus Thioredoxin reductase Mutant C147A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0045454 | biological_process | cell redox homeostasis |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019430 | biological_process | removal of superoxide radicals |
B | 0045454 | biological_process | cell redox homeostasis |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019430 | biological_process | removal of superoxide radicals |
C | 0045454 | biological_process | cell redox homeostasis |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019430 | biological_process | removal of superoxide radicals |
D | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY B1501 |
Chain | Residue |
B | GLY161 |
B | HIS184 |
B | ARG185 |
B | HOH5393 |
B | HOH5603 |
site_id | AC2 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD A2001 |
Chain | Residue |
A | ALA26 |
A | GLY45 |
A | GLU46 |
A | THR47 |
A | GLY50 |
A | GLN51 |
A | GLU54 |
A | ALA55 |
A | VAL58 |
A | ASP60 |
A | ASP90 |
A | ILE91 |
A | VAL92 |
A | GLY120 |
A | ILE121 |
A | GLY122 |
A | VAL123 |
A | TYR143 |
A | CYS144 |
A | ALA147 |
A | GLY286 |
A | ASP287 |
A | ARG296 |
A | GLN297 |
A | VAL298 |
A | HOH5015 |
A | HOH5023 |
A | HOH5028 |
A | HOH5046 |
A | HOH5145 |
A | HOH5636 |
A | GLY22 |
A | LEU23 |
A | GLY24 |
A | PRO25 |
site_id | AC3 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD B2002 |
Chain | Residue |
B | GLY22 |
B | LEU23 |
B | GLY24 |
B | PRO25 |
B | ALA26 |
B | GLY45 |
B | GLU46 |
B | THR47 |
B | GLY50 |
B | GLN51 |
B | GLU54 |
B | ALA55 |
B | ASP60 |
B | ASP90 |
B | ILE91 |
B | VAL92 |
B | GLY120 |
B | ILE121 |
B | GLY122 |
B | TYR143 |
B | ALA147 |
B | GLY286 |
B | ASP287 |
B | ARG296 |
B | GLN297 |
B | VAL298 |
B | HOH5021 |
B | HOH5035 |
B | HOH5041 |
B | HOH5079 |
B | HOH5224 |
B | HOH5511 |
site_id | AC4 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD C2003 |
Chain | Residue |
C | HOH5013 |
C | HOH5064 |
C | HOH5082 |
C | HOH5084 |
C | HOH5546 |
C | GLY22 |
C | LEU23 |
C | GLY24 |
C | PRO25 |
C | ALA26 |
C | GLY45 |
C | GLU46 |
C | THR47 |
C | GLY50 |
C | GLN51 |
C | GLU54 |
C | ALA55 |
C | VAL58 |
C | ASP60 |
C | ASP90 |
C | ILE91 |
C | VAL92 |
C | GLY120 |
C | ILE121 |
C | GLY122 |
C | CYS144 |
C | ALA147 |
C | GLY286 |
C | ASP287 |
C | ARG296 |
C | GLN297 |
C | VAL298 |
site_id | AC5 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD D2004 |
Chain | Residue |
D | GLY22 |
D | LEU23 |
D | GLY24 |
D | PRO25 |
D | ALA26 |
D | GLY45 |
D | GLU46 |
D | THR47 |
D | GLY50 |
D | GLN51 |
D | GLU54 |
D | ALA55 |
D | ASP60 |
D | ASP90 |
D | ILE91 |
D | VAL92 |
D | GLY120 |
D | ILE121 |
D | GLY122 |
D | TYR143 |
D | ALA147 |
D | GLY286 |
D | ASP287 |
D | ARG296 |
D | GLN297 |
D | VAL298 |
D | HOH5003 |
D | HOH5056 |
D | HOH5063 |
D | HOH5076 |
D | HOH5515 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D4162 |
Chain | Residue |
D | GLY163 |
D | ASP164 |
D | SER165 |
D | GLY248 |
D | HOH5477 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B4161 |
Chain | Residue |
B | ASP164 |
B | SER165 |
B | GLY248 |
B | HOH5101 |
B | HOH5481 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C4163 |
Chain | Residue |
C | HIS184 |
C | ARG185 |
C | LYS190 |
D | LYS231 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A4157 |
Chain | Residue |
A | HIS184 |
A | ARG185 |
A | ARG186 |
A | LYS190 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B4158 |
Chain | Residue |
B | HIS184 |
B | ARG185 |
B | ARG186 |
B | LYS190 |
B | HOH5603 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A4159 |
Chain | Residue |
A | ARG126 |
A | GLY163 |
A | ASP164 |
A | SER165 |
A | GLY248 |
A | HOH5133 |
A | HOH5548 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
A | ASP148 | |
A | CYS144 | |
A | ALA147 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
B | ASP148 | |
B | CYS144 | |
B | ALA147 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
C | ASP148 | |
C | CYS144 | |
C | ALA147 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
D | ASP148 | |
D | CYS144 | |
D | ALA147 |