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 |
| 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 |
| 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 |
| 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 |
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 |
