sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.200 Å
X-ray
2012-10-01
| 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 |
|---|---|
| A | 100 % |
| B-Factor: | 87.979 |
|---|---|
| Number of residues: | 35 |
| Including | |
| Standard Amino Acids: | 35 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.864 | 776.250 |
| % Hydrophobic | % Polar |
|---|---|
| 50.00 | 50.00 |
| According to VolSite | |
| HET Code: | XZN |
|---|---|
| Formula: | C26H30Cl2N5O3 |
| Molecular weight: | 531.454 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 53.42 % |
| Polar Surface area: | 84.08 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 7 |
| H-Bond Donors: | 2 |
| Rings: | 4 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 9 |
| X | Y | Z |
|---|---|---|
| -5.86692 | -19.0297 | 20.9745 |
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 |
| CBD | CD1 | LEU- 42 | 3.74 | 0 | Hydrophobic |
| CBC | CD1 | LEU- 42 | 3.7 | 0 | Hydrophobic |
| CAL | CG1 | VAL- 50 | 4.05 | 0 | Hydrophobic |
| CAJ | CG2 | VAL- 50 | 4.34 | 0 | Hydrophobic |
| CAZ | CG1 | VAL- 50 | 3.82 | 0 | Hydrophobic |
| CAK | CB | ALA- 63 | 4.25 | 0 | Hydrophobic |
| CAZ | CB | ALA- 63 | 3.89 | 0 | Hydrophobic |
| CBG | CB | ALA- 63 | 3.57 | 0 | Hydrophobic |
| CBE | CB | ALA- 63 | 3.61 | 0 | Hydrophobic |
| CL2 | CB | LYS- 65 | 3.91 | 0 | Hydrophobic |
| CAX | CD | LYS- 65 | 4.01 | 0 | Hydrophobic |
| C01 | CD | LYS- 65 | 4.49 | 0 | Hydrophobic |
| CAI | CG | LYS- 65 | 4.24 | 0 | Hydrophobic |
| CL2 | CG2 | ILE- 108 | 4.37 | 0 | Hydrophobic |
| C01 | CG2 | ILE- 108 | 4.22 | 0 | Hydrophobic |
| CAZ | CD1 | ILE- 110 | 4.36 | 0 | Hydrophobic |
| CBA | CG2 | ILE- 110 | 4.31 | 0 | Hydrophobic |
| C01 | CD1 | ILE- 110 | 3.62 | 0 | Hydrophobic |
| CL2 | CD1 | ILE- 110 | 3.62 | 0 | Hydrophobic |
| CAN | CE1 | PHE- 112 | 3.74 | 0 | Hydrophobic |
| CAK | CB | CYS- 113 | 4.44 | 0 | Hydrophobic |
| NAT | N | CYS- 113 | 2.93 | 156.51 | H-Bond (Protein Donor) |
| NBI | OE2 | GLU- 124 | 3.71 | 0 | Ionic (Ligand Cationic) |
| CBA | CD1 | LEU- 164 | 3.49 | 0 | Hydrophobic |
| CL1 | CB | ASP- 175 | 4.41 | 0 | Hydrophobic |
