2.100 Å
X-ray
2014-06-05
Name: | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 |
---|---|
ID: | SAMH1_HUMAN |
AC: | Q9Y3Z3 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 3.1.5 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 36.438 |
---|---|
Number of residues: | 35 |
Including | |
Standard Amino Acids: | 32 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.579 | 1080.000 |
% Hydrophobic | % Polar |
---|---|
32.19 | 67.81 |
According to VolSite |
HET Code: | DCP |
---|---|
Formula: | C9H12N3O13P3 |
Molecular weight: | 463.125 g/mol |
DrugBank ID: | DB03258 |
Buried Surface Area: | 64.85 % |
Polar Surface area: | 288.71 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 15 |
H-Bond Donors: | 2 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
7.20939 | 4.21943 | 32.044 |
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 |
O3' | NE2 | GLN- 149 | 2.96 | 163.39 | H-Bond (Protein Donor) |
C2' | CD2 | LEU- 150 | 3.55 | 0 | Hydrophobic |
O4' | NH2 | ARG- 164 | 3.04 | 148.09 | H-Bond (Protein Donor) |
O1A | NH1 | ARG- 164 | 3.12 | 125.39 | H-Bond (Protein Donor) |
O1A | CZ | ARG- 164 | 3.76 | 0 | Ionic (Protein Cationic) |
O2B | NH2 | ARG- 206 | 2.88 | 141.41 | H-Bond (Protein Donor) |
O1A | NE2 | HIS- 210 | 2.9 | 130.99 | H-Bond (Protein Donor) |
O5' | NE2 | HIS- 215 | 2.9 | 136.64 | H-Bond (Protein Donor) |
O1A | NE2 | HIS- 215 | 2.98 | 142.63 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 312 | 2.91 | 162.47 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 312 | 2.91 | 0 | Ionic (Protein Cationic) |
C3' | CD1 | TYR- 315 | 3.64 | 0 | Hydrophobic |
C4' | CD2 | TYR- 315 | 4.08 | 0 | Hydrophobic |
C5' | CE2 | TYR- 315 | 3.44 | 0 | Hydrophobic |
O1G | OH | TYR- 315 | 2.66 | 150.57 | H-Bond (Protein Donor) |
O3' | OD2 | ASP- 319 | 2.56 | 148.69 | H-Bond (Ligand Donor) |
O1G | NE | ARG- 366 | 2.92 | 172.35 | H-Bond (Protein Donor) |
O1G | NH2 | ARG- 366 | 3.48 | 135.14 | H-Bond (Protein Donor) |
O3G | NH2 | ARG- 366 | 3.09 | 142.12 | H-Bond (Protein Donor) |
O1G | CZ | ARG- 366 | 3.66 | 0 | Ionic (Protein Cationic) |
O3G | CZ | ARG- 366 | 3.99 | 0 | Ionic (Protein Cationic) |
C1' | CD1 | TYR- 374 | 4.46 | 0 | Hydrophobic |
C2' | CZ | TYR- 374 | 3.48 | 0 | Hydrophobic |
O2B | MG | MG- 702 | 2.47 | 0 | Metal Acceptor |
O2G | MG | MG- 702 | 2.19 | 0 | Metal Acceptor |
N4 | O | HOH- 855 | 3.16 | 173.14 | H-Bond (Ligand Donor) |