2.100 Å
X-ray
2014-12-11
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: | 30.897 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 34 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.441 | 958.500 |
% Hydrophobic | % Polar |
---|---|
28.52 | 71.48 |
According to VolSite |
HET Code: | DTP |
---|---|
Formula: | C10H12N5O12P3 |
Molecular weight: | 487.150 g/mol |
DrugBank ID: | DB03222 |
Buried Surface Area: | 62.11 % |
Polar Surface area: | 299.64 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
H-Bond Donors: | 2 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
39.6355 | 32.2348 | 24.538 |
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 | 2.92 | 161.37 | H-Bond (Protein Donor) |
C1' | CD2 | LEU- 150 | 3.7 | 0 | Hydrophobic |
O4' | NH2 | ARG- 164 | 3.04 | 145.2 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 312 | 2.77 | 144.67 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 312 | 2.77 | 0 | Ionic (Protein Cationic) |
O1B | OH | TYR- 315 | 3.46 | 170.81 | H-Bond (Protein Donor) |
C5' | CE2 | TYR- 315 | 3.67 | 0 | Hydrophobic |
C4' | CD2 | TYR- 315 | 4.13 | 0 | Hydrophobic |
C3' | CG | TYR- 315 | 3.57 | 0 | Hydrophobic |
C2' | CD1 | TYR- 315 | 4.48 | 0 | Hydrophobic |
O3' | OD2 | ASP- 319 | 2.65 | 173.24 | H-Bond (Ligand Donor) |
O2B | CZ | ARG- 366 | 3.89 | 0 | Ionic (Protein Cationic) |
O2B | NH2 | ARG- 366 | 3.08 | 156.37 | H-Bond (Protein Donor) |
C2' | CZ | TYR- 374 | 3.51 | 0 | Hydrophobic |
O2G | O | HOH- 863 | 2.55 | 179.96 | H-Bond (Protein Donor) |