1.960 Å
X-ray
2009-09-26
Name: | Serine/threonine-protein kinase 24 |
---|---|
ID: | STK24_HUMAN |
AC: | Q9Y6E0 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.7.11.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 45.556 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 31 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.687 | 860.625 |
% Hydrophobic | % Polar |
---|---|
46.67 | 53.33 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 47.52 % |
Polar Surface area: | 319.88 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
7.57485 | 26.2779 | 44.9736 |
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 |
C1' | CG1 | VAL- 38 | 4.07 | 0 | Hydrophobic |
O1A | NZ | LYS- 53 | 3.93 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 53 | 2.84 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 53 | 2.84 | 159.96 | H-Bond (Protein Donor) |
N6 | O | GLU- 100 | 2.81 | 160.4 | H-Bond (Ligand Donor) |
N1 | N | LEU- 102 | 2.9 | 151.8 | H-Bond (Protein Donor) |
C3' | CD2 | LEU- 151 | 4.44 | 0 | Hydrophobic |