2.300 Å
X-ray
2013-02-07
Name: | Nucleocapsid protein |
---|---|
ID: | I6WJ72_9VIRU |
AC: | I6WJ72 |
Organism: | Phlebovirus JS2010-018 |
Reign: | Viruses |
TaxID: | 1205901 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 4 % |
C | 93 % |
D | 4 % |
B-Factor: | 59.485 |
---|---|
Number of residues: | 27 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.092 | 853.875 |
% Hydrophobic | % Polar |
---|---|
49.80 | 50.20 |
According to VolSite |
HET Code: | SVR |
---|---|
Formula: | C51H34N6O23S6 |
Molecular weight: | 1291.232 g/mol |
DrugBank ID: | DB04786 |
Buried Surface Area: | 44.02 % |
Polar Surface area: | 551 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 23 |
H-Bond Donors: | 6 |
Rings: | 8 |
Aromatic rings: | 8 |
Anionic atoms: | 6 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 16 |
X | Y | Z |
---|---|---|
53.0389 | -4.249 | 17.2384 |
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 |
O78 | N | ASN- 66 | 2.87 | 161.94 | H-Bond (Protein Donor) |
C74 | CB | ASN- 66 | 4.23 | 0 | Hydrophobic |
O86 | NH1 | ARG- 95 | 3.32 | 129.99 | H-Bond (Protein Donor) |
O84 | N | ALA- 96 | 3.05 | 151.42 | H-Bond (Protein Donor) |
C70 | CG1 | VAL- 105 | 4.32 | 0 | Hydrophobic |
C56 | CG | PRO- 127 | 4 | 0 | Hydrophobic |
C55 | CB | PRO- 127 | 3.86 | 0 | Hydrophobic |
C70 | CG | MET- 147 | 3.87 | 0 | Hydrophobic |
C67 | CE2 | PHE- 177 | 3.5 | 0 | Hydrophobic |
C62 | CG2 | ILE- 181 | 3.91 | 0 | Hydrophobic |