2.650 Å
X-ray
2009-03-05
Name: | Sensor histidine kinase DesK |
---|---|
ID: | DESK_BACSU |
AC: | O34757 |
Organism: | Bacillus subtilis |
Reign: | Bacteria |
TaxID: | 224308 |
EC Number: | 2.7.13.3 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 99.999 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
1.039 | 550.125 |
% Hydrophobic | % Polar |
---|---|
66.87 | 33.13 |
According to VolSite |
HET Code: | ACP |
---|---|
Formula: | C11H14N5O12P3 |
Molecular weight: | 501.176 g/mol |
DrugBank ID: | DB03909 |
Buried Surface Area: | 60.6 % |
Polar Surface area: | 310.64 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
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 |
---|---|---|
31.0895 | 22.0791 | 28.3584 |
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 |
O3G | MG | MG- 1 | 2.05 | 0 | Metal Acceptor |
O2B | MG | MG- 1 | 2.05 | 0 | Metal Acceptor |
O1A | MG | MG- 1 | 2.06 | 0 | Metal Acceptor |
O1B | NE2 | HIS- 297 | 3.4 | 149.62 | H-Bond (Protein Donor) |
C1' | CE1 | PHE- 324 | 3.58 | 0 | Hydrophobic |
N3 | N | LYS- 325 | 2.62 | 165.25 | H-Bond (Protein Donor) |
C2' | CB | LYS- 325 | 4.07 | 0 | Hydrophobic |
C4' | CB | SER- 330 | 3.38 | 0 | Hydrophobic |
O1G | OG | SER- 332 | 3.41 | 161.77 | H-Bond (Protein Donor) |
O1G | N | GLY- 336 | 2.71 | 152.94 | H-Bond (Protein Donor) |
O1A | N | LEU- 337 | 3.34 | 126.59 | H-Bond (Protein Donor) |
O2A | N | LEU- 337 | 3.29 | 151.68 | H-Bond (Protein Donor) |