sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.380 Å
X-ray
2010-07-16
| Name: | Phenylalanine aminomutase (L-beta-phenylalanine forming) |
|---|---|
| ID: | PAM_TAXCA |
| AC: | Q6GZ04 |
| Organism: | Taxus canadensis |
| Reign: | Eukaryota |
| TaxID: | 88032 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 17 % |
| B | 83 % |
| B-Factor: | 48.021 |
|---|---|
| Number of residues: | 23 |
| Including | |
| Standard Amino Acids: | 22 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.900 | 695.250 |
| % Hydrophobic | % Polar |
|---|---|
| 42.23 | 57.77 |
| According to VolSite | |
| HET Code: | TCA |
|---|---|
| Formula: | C9H7O2 |
| Molecular weight: | 147.151 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 75.79 % |
| Polar Surface area: | 40.12 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 0 |
| Rings: | 1 |
| Aromatic rings: | 1 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 2 |
| X | Y | Z |
|---|---|---|
| -18.8162 | 10.2876 | 26.2133 |
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 |
| C33 | CB | PHE- 86 | 4.01 | 0 | Hydrophobic |
| C33 | CD1 | LEU- 104 | 3.35 | 0 | Hydrophobic |
| C33 | CD1 | LEU- 108 | 4.24 | 0 | Hydrophobic |
| C34 | CD2 | LEU- 108 | 4.35 | 0 | Hydrophobic |
| C34 | CG | LEU- 179 | 4.23 | 0 | Hydrophobic |
| C35 | CD2 | LEU- 179 | 4.38 | 0 | Hydrophobic |
| C32 | CD1 | LEU- 179 | 4.06 | 0 | Hydrophobic |
| C32 | CD2 | LEU- 227 | 4.39 | 0 | Hydrophobic |
| O | NE2 | GLN- 319 | 3.09 | 125.42 | H-Bond (Protein Donor) |
| O | CZ | ARG- 325 | 3.46 | 0 | Ionic (Protein Cationic) |
| O | NH1 | ARG- 325 | 3.27 | 130.09 | H-Bond (Protein Donor) |
| O | NH2 | ARG- 325 | 2.82 | 148.34 | H-Bond (Protein Donor) |
| C35 | CG | GLU- 455 | 4.38 | 0 | Hydrophobic |
