2.300 Å
X-ray
2015-05-19
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 | 45 % |
C | 32 % |
D | 23 % |
B-Factor: | 31.363 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | GTP |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.340 | 2170.125 |
% Hydrophobic | % Polar |
---|---|
43.55 | 56.45 |
According to VolSite |
HET Code: | DTP |
---|---|
Formula: | C10H12N5O12P3 |
Molecular weight: | 487.150 g/mol |
DrugBank ID: | DB03222 |
Buried Surface Area: | 69.35 % |
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 |
---|---|---|
60.0645 | 15.3714 | 127.984 |
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' | N | ASN- 119 | 3.14 | 171.13 | H-Bond (Protein Donor) |
N3 | ND2 | ASN- 119 | 3.07 | 143.67 | H-Bond (Protein Donor) |
C1' | CB | ASN- 119 | 3.65 | 0 | Hydrophobic |
O3' | O | VAL- 156 | 2.67 | 160.52 | H-Bond (Ligand Donor) |
C2' | CG1 | VAL- 156 | 3.57 | 0 | Hydrophobic |
C2' | CZ | PHE- 157 | 3.3 | 0 | Hydrophobic |
C1' | CE2 | PHE- 157 | 3.25 | 0 | Hydrophobic |
O1A | CZ | ARG- 333 | 3.63 | 0 | Ionic (Protein Cationic) |
O1A | NH2 | ARG- 333 | 2.78 | 146.6 | H-Bond (Protein Donor) |
O4' | NH1 | ARG- 333 | 3.05 | 129.91 | H-Bond (Protein Donor) |
DuAr | CZ | ARG- 333 | 3.71 | 30.04 | Pi/Cation |
O1G | NH1 | ARG- 352 | 2.77 | 172.48 | H-Bond (Protein Donor) |
O3G | NH2 | ARG- 352 | 2.68 | 169.92 | H-Bond (Protein Donor) |
O1G | CZ | ARG- 352 | 3.62 | 0 | Ionic (Protein Cationic) |
O3G | CZ | ARG- 352 | 3.62 | 0 | Ionic (Protein Cationic) |
O1G | NZ | LYS- 354 | 3.8 | 0 | Ionic (Protein Cationic) |
O1A | NZ | LYS- 354 | 3.16 | 0 | Ionic (Protein Cationic) |
N6 | OD1 | ASN- 358 | 3.01 | 129.83 | H-Bond (Ligand Donor) |
O1B | NE2 | HIS- 376 | 2.91 | 154 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 523 | 2.81 | 171.12 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 523 | 2.81 | 0 | Ionic (Protein Cationic) |
O3G | NZ | LYS- 523 | 3.46 | 0 | Ionic (Protein Cationic) |
O2G | MG | MG- 701 | 2.14 | 0 | Metal Acceptor |
O2B | MG | MG- 701 | 1.87 | 0 | Metal Acceptor |
O2B | O3' | GTP- 702 | 2.73 | 158.12 | H-Bond (Protein Donor) |
C3' | C1' | GTP- 702 | 4.15 | 0 | Hydrophobic |