sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.000 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: | 26.900 |
|---|---|
| Number of residues: | 38 |
| Including | |
| Standard Amino Acids: | 35 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 2 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.569 | 1397.250 |
| % Hydrophobic | % Polar |
|---|---|
| 57.73 | 42.27 |
| According to VolSite | |
| HET Code: | KTN |
|---|---|
| Formula: | C26H28Cl2N4O4 |
| Molecular weight: | 531.431 g/mol |
| DrugBank ID: | DB01026 |
| Buried Surface Area: | 62 % |
| Polar Surface area: | 69.06 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 6 |
| H-Bond Donors: | 0 |
| Rings: | 5 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 7 |
| X | Y | Z |
|---|---|---|
| -14.6338 | 10.6754 | 14.25 |
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 |
| C26 | CB | PRO- 61 | 4.12 | 0 | Hydrophobic |
| C26 | CD1 | PHE- 72 | 3.36 | 0 | Hydrophobic |
| CL1 | CB | ALA- 74 | 4.01 | 0 | Hydrophobic |
| C23 | CB | ALA- 74 | 3.78 | 0 | Hydrophobic |
| C23 | CE1 | TYR- 75 | 4.24 | 0 | Hydrophobic |
| C21 | CG2 | THR- 92 | 4.42 | 0 | Hydrophobic |
| C19 | CG2 | THR- 92 | 3.71 | 0 | Hydrophobic |
| CL1 | CG2 | ILE- 174 | 3.6 | 0 | Hydrophobic |
| C10 | CG2 | ILE- 174 | 4.37 | 0 | Hydrophobic |
| CL2 | CD2 | LEU- 175 | 3.84 | 0 | Hydrophobic |
| C7 | CG2 | VAL- 237 | 3.91 | 0 | Hydrophobic |
| C20 | CG2 | VAL- 237 | 4.36 | 0 | Hydrophobic |
| C6 | CG1 | VAL- 237 | 3.56 | 0 | Hydrophobic |
| CL2 | CD2 | LEU- 240 | 4.21 | 0 | Hydrophobic |
| C10 | CD2 | LEU- 240 | 3.78 | 0 | Hydrophobic |
| C6 | CB | ALA- 241 | 4.28 | 0 | Hydrophobic |
| C23 | CB | THR- 292 | 4.05 | 0 | Hydrophobic |
| C26 | CG2 | THR- 292 | 4.13 | 0 | Hydrophobic |
| C12 | CD1 | LEU- 391 | 4.45 | 0 | Hydrophobic |
| C10 | CD2 | LEU- 391 | 3.57 | 0 | Hydrophobic |
| O3 | O | HOH- 819 | 3.1 | 179.99 | H-Bond (Protein Donor) |
| O4 | O | HOH- 836 | 2.81 | 152.34 | H-Bond (Protein Donor) |
