sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.600 Å
X-ray
1998-10-23
| Name: | Ferrichrome-iron receptor |
|---|---|
| ID: | FHUA_ECOLI |
| AC: | P06971 |
| Organism: | Escherichia coli |
| Reign: | Bacteria |
| TaxID: | 83333 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 43.659 |
|---|---|
| Number of residues: | 30 |
| Including | |
| Standard Amino Acids: | 29 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.772 | 583.875 |
| % Hydrophobic | % Polar |
|---|---|
| 42.20 | 57.80 |
| According to VolSite | |
| HET Code: | GLY_GLY_GLY_AHO_AHO_AHO_FE |
|---|---|
| Formula: | C25H45N8O11 |
| Molecular weight: | 633.672 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 48.84 % |
| Polar Surface area: | 282.72 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 11 |
| H-Bond Donors: | 8 |
| Rings: | 0 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 21 |
| X | Y | Z |
|---|---|---|
| 113.931 | 46.8542 | 18.5818 |
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 |
| O3 | NH2 | ARG- 81 | 2.97 | 155.96 | H-Bond (Protein Donor) |
| C7 | CE2 | TYR- 87 | 3.87 | 0 | Hydrophobic |
| C7 | CG | GLN- 100 | 4.42 | 0 | Hydrophobic |
| C3 | CB | GLN- 100 | 3.98 | 0 | Hydrophobic |
| C7 | CG | GLN- 100 | 4.2 | 0 | Hydrophobic |
| C4 | CE1 | PHE- 115 | 3.6 | 0 | Hydrophobic |
| C7 | CD1 | TYR- 116 | 3.52 | 0 | Hydrophobic |
| C3 | CZ | TYR- 116 | 3.73 | 0 | Hydrophobic |
| O3 | OH | TYR- 244 | 2.62 | 153.98 | H-Bond (Protein Donor) |
| C3 | CH2 | TRP- 246 | 3.79 | 0 | Hydrophobic |
| C7 | CE2 | TRP- 246 | 3.42 | 0 | Hydrophobic |
| O3 | NE1 | TRP- 246 | 3.44 | 122.95 | H-Bond (Protein Donor) |
| C7 | CG | TYR- 313 | 3.67 | 0 | Hydrophobic |
| C4 | CZ | TYR- 313 | 3.8 | 0 | Hydrophobic |
| O1 | OH | TYR- 315 | 3.24 | 168.23 | H-Bond (Protein Donor) |
| C4 | CE2 | PHE- 391 | 3.94 | 0 | Hydrophobic |
| C7 | CD2 | PHE- 693 | 3.76 | 0 | Hydrophobic |
