sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.000 Å
X-ray
2012-04-19
| Name: | Serine/threonine-protein kinase 10 |
|---|---|
| ID: | STK10_HUMAN |
| AC: | O94804 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 2.7.11.1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| B | 100 % |
| B-Factor: | 49.175 |
|---|---|
| Number of residues: | 39 |
| Including | |
| Standard Amino Acids: | 39 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.455 | 529.875 |
| % Hydrophobic | % Polar |
|---|---|
| 73.25 | 26.75 |
| According to VolSite | |
| HET Code: | G6I |
|---|---|
| Formula: | C30H24F3N7O2 |
| Molecular weight: | 571.552 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 63.1 % |
| Polar Surface area: | 113.95 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 8 |
| H-Bond Donors: | 3 |
| Rings: | 5 |
| Aromatic rings: | 5 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 9 |
| X | Y | Z |
|---|---|---|
| 59.747 | -15.6375 | 53.1778 |
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 |
| CAN | CD1 | LEU- 42 | 4.48 | 0 | Hydrophobic |
| CAR | CD2 | LEU- 42 | 3.97 | 0 | Hydrophobic |
| CAB | CG1 | VAL- 50 | 4.02 | 0 | Hydrophobic |
| CAG | CG1 | VAL- 50 | 3.82 | 0 | Hydrophobic |
| CBO | CB | ALA- 63 | 4.04 | 0 | Hydrophobic |
| CAB | CB | ALA- 63 | 3.81 | 0 | Hydrophobic |
| CAB | CB | LYS- 65 | 3.84 | 0 | Hydrophobic |
| NAZ | OE2 | GLU- 81 | 2.92 | 140.65 | H-Bond (Ligand Donor) |
| CAK | CG | GLU- 81 | 3.7 | 0 | Hydrophobic |
| CAL | CG2 | ILE- 84 | 4.02 | 0 | Hydrophobic |
| CAO | CD1 | LEU- 85 | 4.22 | 0 | Hydrophobic |
| FAD | CD2 | LEU- 85 | 4.36 | 0 | Hydrophobic |
| CBI | CD2 | LEU- 85 | 3.64 | 0 | Hydrophobic |
| FAD | SG | CYS- 88 | 4.15 | 0 | Hydrophobic |
| FAD | CG2 | ILE- 93 | 3.47 | 0 | Hydrophobic |
| CAU | CG2 | VAL- 94 | 3.94 | 0 | Hydrophobic |
| CAM | CG2 | ILE- 108 | 3.76 | 0 | Hydrophobic |
| CBL | CG1 | ILE- 110 | 3.57 | 0 | Hydrophobic |
| CAM | CG1 | ILE- 110 | 3.43 | 0 | Hydrophobic |
| NBA | O | CYS- 113 | 3.04 | 158.08 | H-Bond (Ligand Donor) |
| NAW | N | CYS- 113 | 3.12 | 161.23 | H-Bond (Protein Donor) |
| FAD | CD2 | LEU- 148 | 4.47 | 0 | Hydrophobic |
| FAE | CD1 | LEU- 148 | 3.9 | 0 | Hydrophobic |
| FAF | CG | LEU- 173 | 4.25 | 0 | Hydrophobic |
| OAC | N | ASP- 175 | 2.89 | 171.71 | H-Bond (Protein Donor) |
| CBI | CB | ASP- 175 | 4.06 | 0 | Hydrophobic |
| CAH | CB | SER- 179 | 4.44 | 0 | Hydrophobic |
| FAE | CB | LYS- 181 | 3.9 | 0 | Hydrophobic |
| CAL | CB | LYS- 181 | 3.52 | 0 | Hydrophobic |
