sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.400 Å
X-ray
2009-09-03
| Name: | Transcriptional activator protein LasR |
|---|---|
| ID: | LASR_PSEAE |
| AC: | P25084 |
| Organism: | Pseudomonas aeruginosa |
| Reign: | Bacteria |
| TaxID: | 208964 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 13.448 |
|---|---|
| Number of residues: | 44 |
| Including | |
| Standard Amino Acids: | 41 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 3 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.449 | 401.625 |
| % Hydrophobic | % Polar |
|---|---|
| 63.87 | 36.13 |
| According to VolSite | |
| HET Code: | OHN |
|---|---|
| Formula: | C16H27NO4 |
| Molecular weight: | 297.390 g/mol |
| DrugBank ID: | DB08324 |
| Buried Surface Area: | 79.71 % |
| Polar Surface area: | 72.47 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 1 |
| Rings: | 1 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 11 |
| X | Y | Z |
|---|---|---|
| 10.0237 | 3.45552 | 21.1272 |
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 |
| C13 | CD2 | LEU- 36 | 3.98 | 0 | Hydrophobic |
| C20 | CD1 | LEU- 40 | 4.48 | 0 | Hydrophobic |
| C18 | CD1 | LEU- 40 | 4.08 | 0 | Hydrophobic |
| C20 | CD2 | TYR- 47 | 4.03 | 0 | Hydrophobic |
| C17 | CD2 | TYR- 47 | 4.04 | 0 | Hydrophobic |
| C18 | CB | ALA- 50 | 3.69 | 0 | Hydrophobic |
| C16 | CD1 | ILE- 52 | 3.95 | 0 | Hydrophobic |
| O9 | OH | TYR- 56 | 2.73 | 148.61 | H-Bond (Protein Donor) |
| O6 | NE1 | TRP- 60 | 3.05 | 151.81 | H-Bond (Protein Donor) |
| C13 | CZ | TYR- 64 | 4.02 | 0 | Hydrophobic |
| C14 | CE2 | TYR- 64 | 3.81 | 0 | Hydrophobic |
| N7 | OD2 | ASP- 73 | 2.79 | 167.92 | H-Bond (Ligand Donor) |
| C5 | CG2 | THR- 75 | 4.23 | 0 | Hydrophobic |
| C13 | CG2 | VAL- 76 | 3.96 | 0 | Hydrophobic |
| C10 | CG2 | VAL- 76 | 4.36 | 0 | Hydrophobic |
| C21 | CG1 | VAL- 76 | 4.17 | 0 | Hydrophobic |
| C21 | CB | CYS- 79 | 3.77 | 0 | Hydrophobic |
| C5 | CE2 | TRP- 88 | 3.82 | 0 | Hydrophobic |
| C4 | CE3 | TRP- 88 | 4.18 | 0 | Hydrophobic |
| C4 | CE2 | PHE- 101 | 4.24 | 0 | Hydrophobic |
| C4 | CB | ALA- 105 | 3.85 | 0 | Hydrophobic |
| C4 | CB | LEU- 110 | 4.1 | 0 | Hydrophobic |
| C21 | CG | LEU- 125 | 4.11 | 0 | Hydrophobic |
| C21 | CB | ALA- 127 | 4.25 | 0 | Hydrophobic |
| C19 | CB | ALA- 127 | 4.38 | 0 | Hydrophobic |
| O9 | OG | SER- 129 | 2.7 | 154 | H-Bond (Protein Donor) |
| O12 | O | HOH- 453 | 2.81 | 179.98 | H-Bond (Protein Donor) |
