sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.600 Å
X-ray
2003-08-04
| 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 | 53 % |
| B | 47 % |
| B-Factor: | 31.586 |
|---|---|
| Number of residues: | 40 |
| Including | |
| Standard Amino Acids: | 36 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 4 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.269 | 735.750 |
| % Hydrophobic | % Polar |
|---|---|
| 61.01 | 38.99 |
| According to VolSite | |
| HET Code: | 4CA |
|---|---|
| Formula: | C28H38N7O17P3S |
| Molecular weight: | 869.624 g/mol |
| DrugBank ID: | DB04067 |
| Buried Surface Area: | 53.45 % |
| Polar Surface area: | 432.84 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 22 |
| H-Bond Donors: | 6 |
| Rings: | 4 |
| Aromatic rings: | 3 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 21 |
| X | Y | Z |
|---|---|---|
| 86.1094 | 26.3315 | 22.148 |
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 |
| C2B | CG | GLN- 58 | 3.68 | 0 | Hydrophobic |
| C4B | CB | GLN- 58 | 3.23 | 0 | Hydrophobic |
| C1B | CG | GLU- 73 | 3.66 | 0 | Hydrophobic |
| C3B | CB | MET- 74 | 4.2 | 0 | Hydrophobic |
| C4B | CG | MET- 74 | 3.52 | 0 | Hydrophobic |
| C2B | CB | THR- 77 | 4.39 | 0 | Hydrophobic |
| C7B | CG2 | THR- 77 | 3.7 | 0 | Hydrophobic |
| O2B | OE2 | GLU- 78 | 2.62 | 159.31 | H-Bond (Ligand Donor) |
| C5B | CG | GLU- 78 | 3.82 | 0 | Hydrophobic |
| CDP | CE | MET- 90 | 4.44 | 0 | Hydrophobic |
| CDP | CG2 | VAL- 92 | 4.09 | 0 | Hydrophobic |
| CEP | CG2 | VAL- 92 | 4.24 | 0 | Hydrophobic |
| C6P | CG2 | VAL- 92 | 3.8 | 0 | Hydrophobic |
| S1P | CB | VAL- 92 | 4.24 | 0 | Hydrophobic |
| N4P | O | GLY- 93 | 3.4 | 143.88 | H-Bond (Ligand Donor) |
| CEP | CB | GLN- 94 | 3.75 | 0 | Hydrophobic |
| N8P | O | PHE- 100 | 3.33 | 160.32 | H-Bond (Ligand Donor) |
| C6P | CB | PHE- 100 | 3.78 | 0 | Hydrophobic |
| O3D | NH1 | ARG- 102 | 3.05 | 128.74 | H-Bond (Protein Donor) |
| C1D | CG | PRO- 103 | 4.23 | 0 | Hydrophobic |
| CEP | CB | ALA- 145 | 3.96 | 0 | Hydrophobic |
| N6A | O | PRO- 148 | 2.98 | 150.67 | H-Bond (Ligand Donor) |
| O7A | CZ | ARG- 150 | 3.32 | 0 | Ionic (Protein Cationic) |
| O8A | CZ | ARG- 150 | 3.73 | 0 | Ionic (Protein Cationic) |
| O7A | NH2 | ARG- 150 | 3.3 | 124.72 | H-Bond (Protein Donor) |
| O8A | NH2 | ARG- 150 | 2.81 | 167.51 | H-Bond (Protein Donor) |
| DuAr | CZ | ARG- 150 | 3.92 | 163 | Pi/Cation |
| O5P | O | HOH- 159 | 3.35 | 160.4 | H-Bond (Protein Donor) |
| O2B | O | HOH- 381 | 2.89 | 179.96 | H-Bond (Protein Donor) |
| O4A | O | HOH- 394 | 3.08 | 179.99 | H-Bond (Protein Donor) |
