Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 40 |
Details | binding site for residue FAD A 601 |
Chain | Residue |
A | ILE113 |
A | THR153 |
A | CYS154 |
A | GLY158 |
A | CYS159 |
A | LYS162 |
A | ALA226 |
A | LYS227 |
A | GLY228 |
A | ALA256 |
A | THR257 |
A | GLY114 |
A | GLY258 |
A | TYR296 |
A | VAL297 |
A | ARG393 |
A | VAL400 |
A | GLY432 |
A | ASP433 |
A | GLN440 |
A | LEU441 |
A | THR442 |
A | GLY115 |
A | PRO443 |
A | HIS571 |
A | PRO572 |
A | HOH728 |
A | HOH797 |
A | HOH839 |
A | HOH842 |
A | HOH868 |
A | HOH880 |
A | HOH951 |
A | GLY116 |
A | HOH982 |
A | SER117 |
A | GLY118 |
A | ASP137 |
A | TYR138 |
A | GLY152 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue DVK A 602 |
Chain | Residue |
A | GLY323 |
A | PHE324 |
A | ALA481 |
A | GLY483 |
A | HOH853 |
A | HOH870 |
A | HOH879 |
A | HOH903 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue PGE A 603 |
Chain | Residue |
A | TRP10 |
A | LEU53 |
A | ASN55 |
Functional Information from PROSITE/UniProt
site_id | PS00076 |
Number of Residues | 11 |
Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP |
Chain | Residue | Details |
A | GLY151-PRO161 | |
site_id | PS00194 |
Number of Residues | 19 |
Details | THIOREDOXIN_1 Thioredoxin family active site. VIlFSktTCPYCKkVkdvL |
Chain | Residue | Details |
A | VAL20-LEU38 | |
site_id | PS00195 |
Number of Residues | 17 |
Details | GLUTAREDOXIN_1 Glutaredoxin active site. LFskttCPYCkkVkdvL |
Chain | Residue | Details |
A | LEU22-LEU38 | |