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
1997-11-19
| Name: | Glutathione S-transferase P |
|---|---|
| ID: | GSTP1_HUMAN |
| AC: | P09211 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 2.5.1.18 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 93 % |
| B | 7 % |
| B-Factor: | 9.132 |
|---|---|
| Number of residues: | 33 |
| Including | |
| Standard Amino Acids: | 30 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 3 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.790 | 975.375 |
| % Hydrophobic | % Polar |
|---|---|
| 34.95 | 65.05 |
| According to VolSite | |
| HET Code: | 0HH |
|---|---|
| Formula: | C19H34N3O6S |
| Molecular weight: | 432.555 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 49.93 % |
| Polar Surface area: | 191.4 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 7 |
| H-Bond Donors: | 3 |
| Rings: | 0 |
| Aromatic rings: | 0 |
| Anionic atoms: | 2 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 18 |
| X | Y | Z |
|---|---|---|
| 9.88831 | 5.90483 | 27.9643 |
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 |
| SG | CE1 | TYR- 7 | 3.96 | 0 | Hydrophobic |
| C11 | CZ | TYR- 7 | 4.13 | 0 | Hydrophobic |
| SG | CE2 | PHE- 8 | 3.67 | 0 | Hydrophobic |
| C11 | CD2 | PHE- 8 | 4.29 | 0 | Hydrophobic |
| C3 | CD2 | PHE- 8 | 3.67 | 0 | Hydrophobic |
| C7 | CB | PHE- 8 | 4.03 | 0 | Hydrophobic |
| C6 | CG | PHE- 8 | 3.59 | 0 | Hydrophobic |
| C9 | CG | PRO- 9 | 4.34 | 0 | Hydrophobic |
| C7 | CG1 | VAL- 10 | 3.62 | 0 | Hydrophobic |
| OXT | CZ | ARG- 13 | 3.53 | 0 | Ionic (Protein Cationic) |
| CB | CD | ARG- 13 | 3.77 | 0 | Hydrophobic |
| O2 | NE1 | TRP- 38 | 2.99 | 167.6 | H-Bond (Protein Donor) |
| O2 | NZ | LYS- 44 | 3.32 | 0 | Ionic (Protein Cationic) |
| OXT1 | NZ | LYS- 44 | 3.84 | 0 | Ionic (Protein Cationic) |
| CG | CB | GLN- 51 | 4.4 | 0 | Hydrophobic |
| OXT1 | NE2 | GLN- 51 | 3.03 | 171.09 | H-Bond (Protein Donor) |
| N1 | O | LEU- 52 | 3.02 | 155.96 | H-Bond (Ligand Donor) |
| O1 | N | LEU- 52 | 3.12 | 168.12 | H-Bond (Protein Donor) |
| N | OE1 | GLN- 64 | 2.85 | 136.37 | H-Bond (Ligand Donor) |
| O | N | SER- 65 | 2.84 | 167.3 | H-Bond (Protein Donor) |
| OXT | OG | SER- 65 | 2.78 | 161.63 | H-Bond (Protein Donor) |
| OXT | N | SER- 65 | 3.47 | 137.36 | H-Bond (Protein Donor) |
| N | OD2 | ASP- 98 | 2.72 | 137.81 | H-Bond (Ligand Donor) |
| N | OD2 | ASP- 98 | 2.72 | 0 | Ionic (Ligand Cationic) |
| N | OD1 | ASP- 98 | 3.49 | 0 | Ionic (Ligand Cationic) |
| C2 | CZ | TYR- 108 | 4.08 | 0 | Hydrophobic |
| O | O | HOH- 240 | 2.93 | 147.03 | H-Bond (Protein Donor) |
