sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.800 Å
X-ray
2004-06-01
| Name: | Bifunctional purine biosynthesis protein PURH |
|---|---|
| ID: | PUR9_CHICK |
| AC: | P31335 |
| Organism: | Gallus gallus |
| Reign: | Eukaryota |
| TaxID: | 9031 |
| EC Number: | 2.1.2.3 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 43 % |
| B | 57 % |
| B-Factor: | 30.980 |
|---|---|
| Number of residues: | 29 |
| Including | |
| Standard Amino Acids: | 28 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.686 | 1741.500 |
| % Hydrophobic | % Polar |
|---|---|
| 45.54 | 54.46 |
| According to VolSite | |
| HET Code: | 326 |
|---|---|
| Formula: | C18H12N4O9S2 |
| Molecular weight: | 492.439 g/mol |
| DrugBank ID: | DB03442 |
| Buried Surface Area: | 45.45 % |
| Polar Surface area: | 236.89 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 12 |
| H-Bond Donors: | 0 |
| Rings: | 3 |
| Aromatic rings: | 3 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -11.0877 | -19.7695 | -18.8595 |
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 |
| O32 | NZ | LYS- 267 | 3.32 | 143.33 | H-Bond (Protein Donor) |
| O33 | NZ | LYS- 267 | 2.89 | 145.52 | H-Bond (Protein Donor) |
| O32 | NZ | LYS- 267 | 3.32 | 0 | Ionic (Protein Cationic) |
| O33 | NZ | LYS- 267 | 2.89 | 0 | Ionic (Protein Cationic) |
| C21 | CE | MET- 313 | 4.4 | 0 | Hydrophobic |
| C17 | CE1 | PHE- 316 | 3.76 | 0 | Hydrophobic |
| C21 | CD1 | PHE- 316 | 4.34 | 0 | Hydrophobic |
| C25 | CE2 | PHE- 316 | 3.31 | 0 | Hydrophobic |
| C17 | CG2 | VAL- 338 | 4.07 | 0 | Hydrophobic |
| O32 | CZ | ARG- 452 | 3.57 | 0 | Ionic (Protein Cationic) |
| O34 | N | ARG- 452 | 2.59 | 151.67 | H-Bond (Protein Donor) |
| C29 | CG | ARG- 452 | 4.23 | 0 | Hydrophobic |
| O8 | NZ | LYS- 484 | 3.49 | 0 | Ionic (Protein Cationic) |
| O10 | NZ | LYS- 484 | 3.51 | 0 | Ionic (Protein Cationic) |
| C3 | CB | ALA- 486 | 3.54 | 0 | Hydrophobic |
| N12 | ND2 | ASN- 490 | 2.97 | 144.84 | H-Bond (Protein Donor) |
| C24 | CB | PRO- 544 | 3.66 | 0 | Hydrophobic |
| C29 | CG | PRO- 544 | 3.65 | 0 | Hydrophobic |
