2.800 Å
X-ray
2007-09-09
Name: | Non-structural protein 2 |
---|---|
ID: | NSP2_ROTSR |
AC: | Q03243 |
Organism: | Rotavirus A ) |
Reign: | Viruses |
TaxID: | 36435 |
EC Number: | 3.6.4 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 63.895 |
---|---|
Number of residues: | 24 |
Including | |
Standard Amino Acids: | 23 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.837 | 1292.625 |
% Hydrophobic | % Polar |
---|---|
36.29 | 63.71 |
According to VolSite |
HET Code: | ANP |
---|---|
Formula: | C10H13N6O12P3 |
Molecular weight: | 502.164 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 38.09 % |
Polar Surface area: | 322.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
18.0411 | -43.2395 | 16.4364 |
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 |
C5' | CB | SER- 107 | 4.16 | 0 | Hydrophobic |
O3' | OG | SER- 107 | 3.35 | 159.51 | H-Bond (Ligand Donor) |
O1G | NZ | LYS- 188 | 3.09 | 165.85 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 188 | 3.09 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 223 | 2.81 | 0 | Ionic (Protein Cationic) |
O1G | CZ | ARG- 227 | 3.69 | 0 | Ionic (Protein Cationic) |
O2G | CZ | ARG- 227 | 3.47 | 0 | Ionic (Protein Cationic) |
O1A | CZ | ARG- 227 | 3.9 | 0 | Ionic (Protein Cationic) |
C1' | CD | ARG- 240 | 4.03 | 0 | Hydrophobic |
O3G | O | HOH- 405 | 2.97 | 179.97 | H-Bond (Protein Donor) |