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
2001-07-02
| Name: | 6-deoxyerythronolide B hydroxylase |
|---|---|
| ID: | CPXJ_SACEN |
| AC: | Q00441 |
| Organism: | Saccharopolyspora erythraea |
| Reign: | Bacteria |
| TaxID: | 405948 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 28.649 |
|---|---|
| Number of residues: | 28 |
| Including | |
| Standard Amino Acids: | 26 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.675 | 1296.000 |
| % Hydrophobic | % Polar |
|---|---|
| 56.77 | 43.23 |
| According to VolSite | |
| HET Code: | DEB |
|---|---|
| Formula: | C21H38O6 |
| Molecular weight: | 386.523 g/mol |
| DrugBank ID: | DB04070 |
| Buried Surface Area: | 64.8 % |
| Polar Surface area: | 104.06 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 6 |
| H-Bond Donors: | 3 |
| Rings: | 1 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 1 |
| X | Y | Z |
|---|---|---|
| -13.1167 | 8.71156 | 14.3033 |
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 |
| C14 | CB | ALA- 74 | 3.84 | 0 | Hydrophobic |
| C27 | CB | ALA- 74 | 4.32 | 0 | Hydrophobic |
| C14 | CE2 | TYR- 75 | 4.04 | 0 | Hydrophobic |
| C15 | CZ | PHE- 78 | 4.47 | 0 | Hydrophobic |
| C15 | CD1 | PHE- 86 | 4.44 | 0 | Hydrophobic |
| C25 | CG2 | THR- 92 | 3.54 | 0 | Hydrophobic |
| C15 | CG2 | ILE- 174 | 3.62 | 0 | Hydrophobic |
| C18 | CD2 | LEU- 175 | 3.67 | 0 | Hydrophobic |
| C23 | CG1 | VAL- 237 | 3.9 | 0 | Hydrophobic |
| C18 | CB | LEU- 240 | 4.34 | 0 | Hydrophobic |
| C3 | CB | ALA- 241 | 4.3 | 0 | Hydrophobic |
| C5 | CB | ALA- 241 | 3.83 | 0 | Hydrophobic |
| C23 | CB | ALA- 241 | 3.64 | 0 | Hydrophobic |
| C18 | CG | GLU- 244 | 4.32 | 0 | Hydrophobic |
| C22 | CB | PRO- 288 | 3.85 | 0 | Hydrophobic |
| C15 | CD2 | LEU- 391 | 4.34 | 0 | Hydrophobic |
| C20 | CD1 | LEU- 391 | 3.95 | 0 | Hydrophobic |
| C27 | CD1 | LEU- 391 | 3.8 | 0 | Hydrophobic |
| C20 | CD1 | LEU- 392 | 4.4 | 0 | Hydrophobic |
| O24 | O | HOH- 451 | 2.9 | 179.97 | H-Bond (Protein Donor) |
