sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.800 Å
X-ray
2011-03-15
| Name: | 4-hydroxybenzoyl-CoA thioesterase |
|---|---|
| ID: | 4HBT_ARTSP |
| AC: | Q04416 |
| Organism: | Arthrobacter sp |
| Reign: | Bacteria |
| TaxID: | 1667 |
| EC Number: | 3.1.2.23 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 56 % |
| B | 44 % |
| B-Factor: | 30.499 |
|---|---|
| Number of residues: | 42 |
| Including | |
| Standard Amino Acids: | 39 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 3 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.219 | 924.750 |
| % Hydrophobic | % Polar |
|---|---|
| 54.01 | 45.99 |
| According to VolSite | |
| HET Code: | 4CO |
|---|---|
| Formula: | C29H38N7O18P3S |
| Molecular weight: | 897.634 g/mol |
| DrugBank ID: | DB03613 |
| Buried Surface Area: | 53.89 % |
| Polar Surface area: | 449.91 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 23 |
| H-Bond Donors: | 6 |
| Rings: | 4 |
| Aromatic rings: | 3 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 22 |
| X | Y | Z |
|---|---|---|
| -29.4908 | 71.1928 | 22.9687 |
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 |
| C4B | CB | GLN- 58 | 3.3 | 0 | Hydrophobic |
| C3B | CG | GLN- 58 | 3.58 | 0 | Hydrophobic |
| O1B | N | GLY- 65 | 2.78 | 141.77 | H-Bond (Protein Donor) |
| C3B | CB | MET- 74 | 4.1 | 0 | Hydrophobic |
| C4B | CG | MET- 74 | 3.52 | 0 | Hydrophobic |
| CB | CB | THR- 77 | 4.38 | 0 | Hydrophobic |
| C7B | CB | THR- 77 | 3.63 | 0 | Hydrophobic |
| O2B | OE2 | GLU- 78 | 2.59 | 169.15 | H-Bond (Ligand Donor) |
| C5B | CG | GLU- 78 | 3.86 | 0 | Hydrophobic |
| CDP | CG2 | VAL- 92 | 3.97 | 0 | Hydrophobic |
| CEP | CG2 | VAL- 92 | 4.12 | 0 | Hydrophobic |
| C6P | CB | VAL- 92 | 3.87 | 0 | Hydrophobic |
| S1P | CB | VAL- 92 | 4.13 | 0 | Hydrophobic |
| N4P | O | GLY- 93 | 2.93 | 165.02 | H-Bond (Ligand Donor) |
| CEP | CG | GLN- 94 | 4.16 | 0 | Hydrophobic |
| N8P | O | PHE- 100 | 3.12 | 163.66 | H-Bond (Ligand Donor) |
| C6P | CB | PHE- 100 | 3.92 | 0 | Hydrophobic |
| C4D | CG | ARG- 102 | 4.47 | 0 | Hydrophobic |
| C1D | CG | PRO- 103 | 4.41 | 0 | Hydrophobic |
| CEP | CB | ALA- 145 | 3.98 | 0 | Hydrophobic |
| CDP | CG | ARG- 147 | 4.34 | 0 | Hydrophobic |
| N6A | O | PRO- 148 | 3.1 | 150.44 | H-Bond (Ligand Donor) |
| O7A | NH1 | ARG- 150 | 3.15 | 168.31 | H-Bond (Protein Donor) |
| O8A | NH2 | ARG- 150 | 2.81 | 171.71 | H-Bond (Protein Donor) |
| O8A | NH1 | ARG- 150 | 3.45 | 131.85 | H-Bond (Protein Donor) |
| O8A | CZ | ARG- 150 | 3.57 | 0 | Ionic (Protein Cationic) |
| DuAr | CZ | ARG- 150 | 3.94 | 164.8 | Pi/Cation |
| O2B | O | HOH- 504 | 2.95 | 179.98 | H-Bond (Protein Donor) |
| O5P | O | HOH- 929 | 3 | 156.31 | H-Bond (Protein Donor) |
