sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.400 Å
X-ray
2011-01-16
| Name: | Receptor-type tyrosine-protein phosphatase gamma |
|---|---|
| ID: | PTPRG_HUMAN |
| AC: | P23470 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 3.1.3.48 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 47.469 |
|---|---|
| Number of residues: | 28 |
| Including | |
| Standard Amino Acids: | 28 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.270 | 482.625 |
| % Hydrophobic | % Polar |
|---|---|
| 65.03 | 34.97 |
| According to VolSite | |
| HET Code: | NX2 |
|---|---|
| Formula: | C13H11Cl2NO3S3 |
| Molecular weight: | 396.332 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 65.56 % |
| Polar Surface area: | 125.16 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: | 5 |
| X | Y | Z |
|---|---|---|
| 20.1042 | 30.1935 | 60.6668 |
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 |
| CL14 | CG2 | ILE- 950 | 3.69 | 0 | Hydrophobic |
| CL15 | CD1 | ILE- 950 | 4.37 | 0 | Hydrophobic |
| C13 | CG2 | ILE- 950 | 3.6 | 0 | Hydrophobic |
| CL14 | CG | TYR- 1023 | 3.97 | 0 | Hydrophobic |
| S6 | CZ3 | TRP- 1026 | 3.96 | 0 | Hydrophobic |
| C11 | CH2 | TRP- 1026 | 3.3 | 0 | Hydrophobic |
| S4 | CG2 | VAL- 1031 | 3.53 | 0 | Hydrophobic |
| S6 | CG | PRO- 1032 | 3.75 | 0 | Hydrophobic |
| C11 | CG | PRO- 1032 | 4.15 | 0 | Hydrophobic |
| CL15 | CG1 | VAL- 1038 | 3.84 | 0 | Hydrophobic |
| C10 | CG2 | VAL- 1038 | 3.53 | 0 | Hydrophobic |
| C13 | CG1 | VAL- 1038 | 3.56 | 0 | Hydrophobic |
| CL14 | CD2 | PHE- 1041 | 3.34 | 0 | Hydrophobic |
| S6 | CG | ARG- 1066 | 3.98 | 0 | Hydrophobic |
| O18 | NE | ARG- 1066 | 3.05 | 160.11 | H-Bond (Protein Donor) |
| O21 | NH1 | ARG- 1066 | 2.96 | 146.37 | H-Bond (Protein Donor) |
| CL15 | CG2 | THR- 1069 | 3.95 | 0 | Hydrophobic |
| C9 | CG2 | THR- 1069 | 3.6 | 0 | Hydrophobic |
| CL15 | CB | TYR- 1070 | 3.64 | 0 | Hydrophobic |
| CL15 | CD1 | ILE- 1073 | 4.44 | 0 | Hydrophobic |
| C20 | CG2 | THR- 1105 | 4.5 | 0 | Hydrophobic |
| S4 | CB | GLU- 1107 | 3.74 | 0 | Hydrophobic |
| S4 | CG | GLN- 1108 | 3.94 | 0 | Hydrophobic |
| O18 | NE2 | GLN- 1108 | 3.42 | 165.92 | H-Bond (Protein Donor) |
| C7 | CE2 | PHE- 1111 | 3.61 | 0 | Hydrophobic |
