sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.100 Å
X-ray
2012-02-17
| Name: | Genome polyprotein |
|---|---|
| ID: | POLG_HCVJ4 |
| AC: | O92972 |
| Organism: | Hepatitis C virus genotype 1b |
| Reign: | Viruses |
| TaxID: | 420174 |
| EC Number: | 2.7.7.48 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 64.747 |
|---|---|
| Number of residues: | 31 |
| Including | |
| Standard Amino Acids: | 31 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.329 | 405.000 |
| % Hydrophobic | % Polar |
|---|---|
| 61.67 | 38.33 |
| According to VolSite | |
| HET Code: | 0LN |
|---|---|
| Formula: | C32H38N4O5S |
| Molecular weight: | 590.733 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 50.19 % |
| Polar Surface area: | 109.33 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 1 |
| Rings: | 6 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 2 |
| X | Y | Z |
|---|---|---|
| 79.1226 | -14.5815 | -30.4029 |
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 |
| C26 | CB | MET- 36 | 4.08 | 0 | Hydrophobic |
| C26 | CB | VAL- 37 | 3.69 | 0 | Hydrophobic |
| C26 | SG | CYS- 146 | 4.31 | 0 | Hydrophobic |
| C14 | CD2 | LEU- 392 | 3.65 | 0 | Hydrophobic |
| C26 | CB | ALA- 393 | 4.35 | 0 | Hydrophobic |
| C12 | CB | ALA- 395 | 3.45 | 0 | Hydrophobic |
| C11 | CB | ALA- 396 | 4.04 | 0 | Hydrophobic |
| C17 | CB | ALA- 396 | 3.51 | 0 | Hydrophobic |
| C14 | CG2 | ILE- 424 | 3.76 | 0 | Hydrophobic |
| C14 | CD1 | LEU- 425 | 4.2 | 0 | Hydrophobic |
| C13 | CB | HIS- 428 | 4.27 | 0 | Hydrophobic |
| C13 | CE2 | PHE- 429 | 4.13 | 0 | Hydrophobic |
| C12 | CZ | PHE- 429 | 4.47 | 0 | Hydrophobic |
| C26 | CG | LEU- 492 | 3.78 | 0 | Hydrophobic |
| C21 | CB | LEU- 492 | 4.41 | 0 | Hydrophobic |
| C22 | CG | LEU- 492 | 3.77 | 0 | Hydrophobic |
| C4 | CG2 | VAL- 494 | 4.43 | 0 | Hydrophobic |
| C10 | CG2 | VAL- 494 | 4.49 | 0 | Hydrophobic |
| C15 | CG1 | VAL- 494 | 4.19 | 0 | Hydrophobic |
| C21 | CG2 | VAL- 494 | 3.69 | 0 | Hydrophobic |
| C1 | CG | PRO- 495 | 4.17 | 0 | Hydrophobic |
| C15 | CZ2 | TRP- 500 | 4.43 | 0 | Hydrophobic |
| O33 | NH2 | ARG- 503 | 2.94 | 138.43 | H-Bond (Protein Donor) |
| O28 | NH2 | ARG- 503 | 2.86 | 126.16 | H-Bond (Protein Donor) |
| O28 | NH1 | ARG- 503 | 2.9 | 125.28 | H-Bond (Protein Donor) |
