sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.340 Å
X-ray
2010-06-04
| Name: | Ketohexokinase |
|---|---|
| ID: | KHK_HUMAN |
| AC: | P50053 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 44.507 |
|---|---|
| Number of residues: | 27 |
| Including | |
| Standard Amino Acids: | 26 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.604 | 722.250 |
| % Hydrophobic | % Polar |
|---|---|
| 42.99 | 57.01 |
| According to VolSite | |
| HET Code: | TR4 |
|---|---|
| Formula: | C11H10N4S |
| Molecular weight: | 230.289 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 65.24 % |
| Polar Surface area: | 92.93 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 1 |
| Rings: | 2 |
| Aromatic rings: | 2 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 2 |
| X | Y | Z |
|---|---|---|
| -3.12662 | -1.59825 | 18.3481 |
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 |
| C01 | CB | ALA- 224 | 4.29 | 0 | Hydrophobic |
| C15 | CB | GLU- 227 | 3.7 | 0 | Hydrophobic |
| C01 | CB | ALA- 230 | 4.08 | 0 | Hydrophobic |
| C16 | CB | ALA- 244 | 3.86 | 0 | Hydrophobic |
| C15 | CB | PRO- 246 | 3.58 | 0 | Hydrophobic |
| C13 | CG2 | VAL- 250 | 3.93 | 0 | Hydrophobic |
| S02 | CD1 | PHE- 260 | 3.8 | 0 | Hydrophobic |
| C01 | SG | CYS- 282 | 3.34 | 0 | Hydrophobic |
| S02 | CB | ALA- 285 | 3.79 | 0 | Hydrophobic |
| C13 | CB | CYS- 289 | 4.07 | 0 | Hydrophobic |
| C12 | SG | CYS- 289 | 3.43 | 0 | Hydrophobic |
| N04 | O | HOH- 304 | 2.85 | 152.93 | H-Bond (Protein Donor) |
