1.800 Å
X-ray
2015-03-05
Name: | Tankyrase-2 |
---|---|
ID: | TNKS2_HUMAN |
AC: | Q9H2K2 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.4.2.30 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 26.198 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.791 | 340.875 |
% Hydrophobic | % Polar |
---|---|
58.42 | 41.58 |
According to VolSite |
HET Code: | 29F |
---|---|
Formula: | C18H18N2O |
Molecular weight: | 278.348 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 75.34 % |
Polar Surface area: | 41.46 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 1 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
-54.3 | -42.9495 | 17.8674 |
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 |
N | O | GLY- 1032 | 2.9 | 152.68 | H-Bond (Ligand Donor) |
O | N | GLY- 1032 | 2.88 | 173.13 | H-Bond (Protein Donor) |
C9 | CB | SER- 1033 | 3.91 | 0 | Hydrophobic |
C | CG | PRO- 1034 | 4.15 | 0 | Hydrophobic |
C3 | CE2 | PHE- 1035 | 3.6 | 0 | Hydrophobic |
C6 | CB | TYR- 1050 | 3.64 | 0 | Hydrophobic |
C16 | CB | TYR- 1060 | 3.37 | 0 | Hydrophobic |
C14 | CB | ALA- 1062 | 3.66 | 0 | Hydrophobic |
C14 | CG | LYS- 1067 | 3.59 | 0 | Hydrophobic |
O | OG | SER- 1068 | 2.9 | 155.99 | H-Bond (Protein Donor) |
C7 | CB | TYR- 1071 | 4.01 | 0 | Hydrophobic |
C2 | CD1 | ILE- 1075 | 3.79 | 0 | Hydrophobic |
C5 | CG1 | ILE- 1075 | 4.04 | 0 | Hydrophobic |
C14 | CG | GLU- 1138 | 3.97 | 0 | Hydrophobic |