2.300 Å
X-ray
2014-05-22
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: | 40.843 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 36 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.227 | 826.875 |
% Hydrophobic | % Polar |
---|---|
30.61 | 69.39 |
According to VolSite |
HET Code: | TTP |
---|---|
Formula: | C10H13N2O14P3 |
Molecular weight: | 478.137 g/mol |
DrugBank ID: | DB02452 |
Buried Surface Area: | 64.04 % |
Polar Surface area: | 279.44 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
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 |
---|---|---|
-20.1121 | 3.48117 | 42.7125 |
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 | 3.36 | 156.88 | H-Bond (Protein Donor) |
C2' | CD2 | LEU- 150 | 3.54 | 0 | Hydrophobic |
O2A | NH1 | ARG- 164 | 3.31 | 132.6 | H-Bond (Protein Donor) |
O4' | NH2 | ARG- 164 | 3.39 | 137.15 | H-Bond (Protein Donor) |
O1B | NH2 | ARG- 206 | 3.22 | 168.98 | H-Bond (Protein Donor) |
O2A | NE2 | HIS- 210 | 2.73 | 132.41 | H-Bond (Protein Donor) |
O2A | NE2 | HIS- 215 | 3.2 | 136.03 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 312 | 2.82 | 155.4 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 312 | 2.82 | 0 | Ionic (Protein Cationic) |
O2G | NZ | LYS- 312 | 3.85 | 0 | Ionic (Protein Cationic) |
O2G | OH | TYR- 315 | 2.62 | 142.69 | H-Bond (Protein Donor) |
C5' | CD2 | TYR- 315 | 3.91 | 0 | Hydrophobic |
C3' | CD1 | TYR- 315 | 3.76 | 0 | Hydrophobic |
O3' | OD2 | ASP- 319 | 2.56 | 129.83 | H-Bond (Ligand Donor) |
O2G | NE | ARG- 366 | 2.81 | 177.91 | H-Bond (Protein Donor) |
O3G | NH2 | ARG- 366 | 2.95 | 162.55 | H-Bond (Protein Donor) |
O2G | CZ | ARG- 366 | 3.65 | 0 | Ionic (Protein Cationic) |
O3G | CZ | ARG- 366 | 3.82 | 0 | Ionic (Protein Cationic) |
C5M | CB | TYR- 374 | 4.41 | 0 | Hydrophobic |
C2' | CZ | TYR- 374 | 3.68 | 0 | Hydrophobic |
O4 | NE2 | GLN- 375 | 3.04 | 127.08 | H-Bond (Protein Donor) |
O1B | MG | MG- 705 | 2.26 | 0 | Metal Acceptor |
O1G | MG | MG- 705 | 2.13 | 0 | Metal Acceptor |