6BU7
Crystal structure of Trypanothione Reductase from Trypanosoma brucei in complex with inhibitor RD130 1-[2-(Piperidin-4-yl)ethyl]-5-{5-[1-(pyrrolidin-1-yl)cyclohexyl]-1,3-thiazol-2-yl}-1H-indole
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 | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0015036 | molecular_function | disulfide oxidoreductase activity |
A | 0015042 | molecular_function | trypanothione-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 | 0020015 | cellular_component | glycosome |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0097014 | cellular_component | ciliary plasm |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0015036 | molecular_function | disulfide oxidoreductase activity |
B | 0015042 | molecular_function | trypanothione-disulfide reductase (NADPH) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
B | 0020015 | cellular_component | glycosome |
B | 0045454 | biological_process | cell redox homeostasis |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0097014 | cellular_component | ciliary plasm |
B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 30 |
Details | binding site for residue FAD A 501 |
Chain | Residue |
A | ILE10 |
A | ALA47 |
A | GLY50 |
A | THR51 |
A | CYS52 |
A | LYS60 |
A | TRP126 |
A | GLY127 |
A | ALA159 |
A | THR160 |
A | GLY161 |
A | GLY11 |
A | ILE199 |
A | ARG290 |
A | GLY326 |
A | ASP327 |
A | MET333 |
A | LEU334 |
A | THR335 |
A | PRO336 |
A | ALA338 |
A | HOH603 |
A | GLY13 |
B | HIS461 |
A | SER14 |
A | GLY15 |
A | VAL34 |
A | ASP35 |
A | VAL36 |
A | ALA46 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | GLY197 |
A | PHE198 |
A | GLY286 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | TYR221 |
A | ARG222 |
A | ASN223 |
A | ARG228 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | LYS257 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue RD0 A 505 |
Chain | Residue |
A | TRP21 |
A | TYR110 |
A | ASP116 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 506 |
Chain | Residue |
A | ARG138 |
A | GLN152 |
site_id | AC7 |
Number of Residues | 30 |
Details | binding site for residue FAD B 501 |
Chain | Residue |
A | HIS461 |
A | PRO462 |
B | ILE10 |
B | GLY11 |
B | GLY13 |
B | SER14 |
B | GLY15 |
B | VAL34 |
B | ASP35 |
B | ALA46 |
B | ALA47 |
B | GLY50 |
B | THR51 |
B | CYS52 |
B | GLY56 |
B | CYS57 |
B | LYS60 |
B | TRP126 |
B | GLY127 |
B | ALA159 |
B | THR160 |
B | GLY161 |
B | ARG287 |
B | ARG290 |
B | GLY326 |
B | ASP327 |
B | MET333 |
B | LEU334 |
B | THR335 |
B | PRO336 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | LYS257 |
B | SER259 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue EPE B 503 |
Chain | Residue |
B | ASN91 |
B | LYS93 |
B | TRP126 |
B | THR140 |
B | ALA141 |
B | TRP163 |
B | ARG290 |
B | ASN292 |
B | ASP293 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue RD0 B 504 |
Chain | Residue |
B | TRP21 |
B | SER109 |
B | MET113 |
B | ASP116 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EPE B 505 |
Chain | Residue |
B | TYR221 |
B | ARG222 |
B | ASN223 |
B | GLY286 |
B | HOH605 |
B | HOH606 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | ARG189 |
B | ARG190 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GOL B 507 |
Chain | Residue |
A | ASN456 |
A | ARG472 |
B | ARG355 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 509 |
Chain | Residue |
B | ASN224 |
B | LEU225 |
B | ARG228 |
B | ARG235 |
Functional Information from PROSITE/UniProt
site_id | PS00076 |
Number of Residues | 11 |
Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP |
Chain | Residue | Details |
A | GLY49-PRO59 |