sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.320 Å
X-ray
2010-11-25
| Name: | Putative oxidoreductase |
|---|---|
| ID: | Q7X2G7_9ACTN |
| AC: | Q7X2G7 |
| Organism: | Streptomyces griseoflavus |
| Reign: | Bacteria |
| TaxID: | 35619 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| C | 100 % |
| B-Factor: | 25.982 |
|---|---|
| Number of residues: | 42 |
| Including | |
| Standard Amino Acids: | 41 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | FAD |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.394 | 1346.625 |
| % Hydrophobic | % Polar |
|---|---|
| 52.38 | 47.62 |
| According to VolSite | |
| HET Code: | VGP |
|---|---|
| Formula: | C27H28O9 |
| Molecular weight: | 496.506 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 71.71 % |
| Polar Surface area: | 138.07 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 9 |
| H-Bond Donors: | 5 |
| Rings: | 5 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 5 |
| X | Y | Z |
|---|---|---|
| 27.6478 | -6.68903 | 100.707 |
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 |
| C | CB | ALA- 124 | 4.3 | 0 | Hydrophobic |
| C15 | CB | ALA- 124 | 3.37 | 0 | Hydrophobic |
| C15 | CB | ALA- 124 | 3.37 | 0 | Hydrophobic |
| C07 | SG | CYS- 125 | 3.46 | 0 | Hydrophobic |
| C07 | SG | CYS- 125 | 3.46 | 0 | Hydrophobic |
| C19 | CE2 | TYR- 139 | 3.7 | 0 | Hydrophobic |
| C19 | CG | PRO- 141 | 4.19 | 0 | Hydrophobic |
| C18 | CZ | PHE- 265 | 3.32 | 0 | Hydrophobic |
| C | CG2 | THR- 267 | 4.37 | 0 | Hydrophobic |
| C16 | CG2 | THR- 267 | 4.38 | 0 | Hydrophobic |
| C | CZ | PHE- 269 | 3.73 | 0 | Hydrophobic |
| C26 | CZ | PHE- 269 | 4.01 | 0 | Hydrophobic |
| C | CE | MET- 281 | 3.67 | 0 | Hydrophobic |
| C09 | CB | GLN- 328 | 4.41 | 0 | Hydrophobic |
| C10 | CG | GLN- 328 | 4.27 | 0 | Hydrophobic |
| C26 | CG | GLN- 328 | 3.89 | 0 | Hydrophobic |
| O07 | OG | SER- 341 | 3.26 | 158.05 | H-Bond (Ligand Donor) |
| C22 | CB | SER- 341 | 3.86 | 0 | Hydrophobic |
| C24 | CB | SER- 341 | 4.3 | 0 | Hydrophobic |
| C08 | CE | MET- 374 | 3.7 | 0 | Hydrophobic |
| C13 | SD | MET- 374 | 3.6 | 0 | Hydrophobic |
| O07 | OG | SER- 402 | 2.9 | 134.06 | H-Bond (Protein Donor) |
| O08 | OG | SER- 402 | 3.13 | 160.18 | H-Bond (Ligand Donor) |
| C11 | CZ | TYR- 448 | 4.46 | 0 | Hydrophobic |
| C20 | CE2 | TYR- 448 | 3.81 | 0 | Hydrophobic |
| C23 | CD2 | TYR- 448 | 3.76 | 0 | Hydrophobic |
| C21 | C9A | FAD- 499 | 3.46 | 0 | Hydrophobic |
| C23 | C9 | FAD- 499 | 4 | 0 | Hydrophobic |
| C24 | C8M | FAD- 499 | 4.46 | 0 | Hydrophobic |
| C11 | C6 | FAD- 499 | 4.18 | 0 | Hydrophobic |
| C02 | C7M | FAD- 499 | 3.58 | 0 | Hydrophobic |
