1.850 Å
X-ray
2013-06-05
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 | 93 % |
C | 7 % |
B-Factor: | 19.738 |
---|---|
Number of residues: | 29 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.012 | 438.750 |
% Hydrophobic | % Polar |
---|---|
53.85 | 46.15 |
According to VolSite |
HET Code: | 1VF |
---|---|
Formula: | C21H21N2O3 |
Molecular weight: | 349.403 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 67.9 % |
Polar Surface area: | 51.05 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 1 |
Rings: | 4 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
6.32815 | -37.4603 | -9.80727 |
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 |
OAS | N | GLY- 1032 | 2.95 | 163.66 | H-Bond (Protein Donor) |
CAN | CB | SER- 1033 | 4.18 | 0 | Hydrophobic |
CAK | CB | TYR- 1050 | 4.23 | 0 | Hydrophobic |
CAX | CB | TYR- 1060 | 3.36 | 0 | Hydrophobic |
CAU | CB | ALA- 1062 | 3.69 | 0 | Hydrophobic |
CAV | CG | LYS- 1067 | 3.48 | 0 | Hydrophobic |
OAS | OG | SER- 1068 | 2.9 | 162 | H-Bond (Protein Donor) |
CAL | CD1 | TYR- 1071 | 3.37 | 0 | Hydrophobic |
CAN | CB | TYR- 1071 | 3.78 | 0 | Hydrophobic |
CAK | CG1 | ILE- 1075 | 3.77 | 0 | Hydrophobic |
CAV | CG | GLU- 1138 | 4.16 | 0 | Hydrophobic |