sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.370 Å
X-ray
2009-08-13
| Name: | Bifunctional dihydrofolate reductase-thymidylate synthase |
|---|---|
| ID: | DRTS_TRYCR |
| AC: | Q27793 |
| Organism: | Trypanosoma cruzi |
| Reign: | Eukaryota |
| TaxID: | 5693 |
| EC Number: | 1.5.1.3 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 25.000 |
|---|---|
| Number of residues: | 26 |
| Including | |
| Standard Amino Acids: | 25 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | NDP |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.492 | 624.375 |
| % Hydrophobic | % Polar |
|---|---|
| 63.78 | 36.22 |
| According to VolSite | |
| HET Code: | C50 |
|---|---|
| Formula: | C14H21Cl2N5O2 |
| Molecular weight: | 362.255 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 65.91 % |
| Polar Surface area: | 101.68 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 4 |
| Rings: | 2 |
| Aromatic rings: | 1 |
| Anionic atoms: | 0 |
| Cationic atoms: | 2 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -33.302 | 16.062 | 54.7359 |
Image generated by PoseView
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
| Ligand | Protein | Interaction | |||
|---|---|---|---|---|---|
| Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
| N8 | O | VAL- 26 | 2.77 | 166.56 | H-Bond (Ligand Donor) |
| C23 | CB | ALA- 28 | 3.95 | 0 | Hydrophobic |
| C12 | CD1 | ILE- 41 | 4.29 | 0 | Hydrophobic |
| C19 | CD1 | ILE- 41 | 4.45 | 0 | Hydrophobic |
| C23 | CD1 | ILE- 41 | 3.49 | 0 | Hydrophobic |
| N1 | OD2 | ASP- 48 | 2.71 | 148.04 | H-Bond (Protein Donor) |
| N7 | OD2 | ASP- 48 | 3.47 | 124.8 | H-Bond (Ligand Donor) |
| N7 | OD1 | ASP- 48 | 2.77 | 163.79 | H-Bond (Ligand Donor) |
| C17 | CE | MET- 49 | 4.38 | 0 | Hydrophobic |
| CL20 | SD | MET- 49 | 3.85 | 0 | Hydrophobic |
| C22 | SD | MET- 49 | 3.64 | 0 | Hydrophobic |
| C16 | SD | MET- 49 | 3.86 | 0 | Hydrophobic |
| C10 | CE2 | PHE- 52 | 3.69 | 0 | Hydrophobic |
| CL20 | CE1 | PHE- 52 | 4.16 | 0 | Hydrophobic |
| C22 | CG | PHE- 52 | 3.89 | 0 | Hydrophobic |
| C11 | CG2 | THR- 80 | 3.47 | 0 | Hydrophobic |
| CL20 | CD1 | ILE- 84 | 4.49 | 0 | Hydrophobic |
| C16 | CG2 | ILE- 84 | 4.17 | 0 | Hydrophobic |
| C14 | CG1 | ILE- 84 | 3.97 | 0 | Hydrophobic |
| CL21 | CD2 | PHE- 88 | 3.62 | 0 | Hydrophobic |
| CL20 | CD2 | LEU- 91 | 3.88 | 0 | Hydrophobic |
| N8 | O | ILE- 154 | 2.79 | 150.08 | H-Bond (Ligand Donor) |
| C10 | CB | ILE- 154 | 4.36 | 0 | Hydrophobic |
| C11 | CD1 | ILE- 154 | 4.39 | 0 | Hydrophobic |
| C10 | C4N | NDP- 602 | 4.19 | 0 | Hydrophobic |
| C23 | C3N | NDP- 602 | 4.41 | 0 | Hydrophobic |
| C11 | C5N | NDP- 602 | 3.67 | 0 | Hydrophobic |
