sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.900 Å
X-ray
2006-10-26
| Name: | Modification methylase TaqI |
|---|---|
| ID: | MTTA_THEAQ |
| AC: | P14385 |
| Organism: | Thermus aquaticus |
| Reign: | Bacteria |
| TaxID: | 271 |
| EC Number: | 2.1.1.72 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 16.557 |
|---|---|
| Number of residues: | 32 |
| Including | |
| Standard Amino Acids: | 31 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.086 | 614.250 |
| % Hydrophobic | % Polar |
|---|---|
| 57.69 | 42.31 |
| According to VolSite | |
| HET Code: | NEA |
|---|---|
| Formula: | C12H19N6O3S |
| Molecular weight: | 327.383 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 60.57 % |
| Polar Surface area: | 172.25 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 8 |
| H-Bond Donors: | 4 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 5 |
| X | Y | Z |
|---|---|---|
| -49.5549 | 1.61891 | 14.798 |
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 |
| CG | CA | VAL- 21 | 3.46 | 0 | Hydrophobic |
| C5' | CG1 | VAL- 21 | 3.59 | 0 | Hydrophobic |
| N | O | ALA- 47 | 2.76 | 146.18 | H-Bond (Ligand Donor) |
| SD | CB | ALA- 47 | 4.21 | 0 | Hydrophobic |
| C4' | CB | ALA- 47 | 4.19 | 0 | Hydrophobic |
| C1' | CB | ALA- 47 | 3.91 | 0 | Hydrophobic |
| O3' | OE1 | GLU- 71 | 2.83 | 159.81 | H-Bond (Ligand Donor) |
| O2' | OE2 | GLU- 71 | 2.57 | 157.99 | H-Bond (Ligand Donor) |
| C1' | CG2 | ILE- 72 | 4.35 | 0 | Hydrophobic |
| N3 | N | ILE- 72 | 3.34 | 128.05 | H-Bond (Protein Donor) |
| N6 | OD1 | ASP- 89 | 2.94 | 154.61 | H-Bond (Ligand Donor) |
| N1 | N | PHE- 90 | 2.95 | 166.11 | H-Bond (Protein Donor) |
| N | O | ASN- 105 | 2.83 | 161.65 | H-Bond (Ligand Donor) |
| SD | CB | PRO- 107 | 4 | 0 | Hydrophobic |
