1.900 Å
X-ray
2006-10-02
Name: | AGAP009194-PA |
---|---|
ID: | Q7PVS6_ANOGA |
AC: | Q7PVS6 |
Organism: | Anopheles gambiae |
Reign: | Eukaryota |
TaxID: | 7165 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 18 % |
B | 82 % |
B-Factor: | 21.205 |
---|---|
Number of residues: | 39 |
Including | |
Standard Amino Acids: | 39 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.032 | 843.750 |
% Hydrophobic | % Polar |
---|---|
65.60 | 34.40 |
According to VolSite |
HET Code: | GTX |
---|---|
Formula: | C16H28N3O6S |
Molecular weight: | 390.475 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 59.25 % |
Polar Surface area: | 191.4 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 3 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 15 |
X | Y | Z |
---|---|---|
4.08435 | 13.031 | 30.0052 |
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 |
C6S | CD2 | LEU- 9 | 4.05 | 0 | Hydrophobic |
C6S | CD2 | LEU- 11 | 3.57 | 0 | Hydrophobic |
SG2 | CB | SER- 12 | 4.27 | 0 | Hydrophobic |
C4S | CB | SER- 12 | 4.14 | 0 | Hydrophobic |
CG1 | CG | PRO- 14 | 3.92 | 0 | Hydrophobic |
SG2 | CG | PRO- 14 | 3.83 | 0 | Hydrophobic |
CB2 | CD1 | LEU- 36 | 3.68 | 0 | Hydrophobic |
C3S | CD1 | LEU- 36 | 3.85 | 0 | Hydrophobic |
O31 | ND1 | HIS- 53 | 3.09 | 137.5 | H-Bond (Protein Donor) |
CG1 | CB | THR- 54 | 3.82 | 0 | Hydrophobic |
N2 | O | ILE- 55 | 3.16 | 147.29 | H-Bond (Ligand Donor) |
O2 | N | ILE- 55 | 2.96 | 161.07 | H-Bond (Protein Donor) |
CB2 | CG1 | ILE- 55 | 4.18 | 0 | Hydrophobic |
N1 | OE1 | GLU- 67 | 2.79 | 156.87 | H-Bond (Ligand Donor) |
N1 | OE1 | GLU- 67 | 2.79 | 0 | Ionic (Ligand Cationic) |
O11 | N | SER- 68 | 2.94 | 167.47 | H-Bond (Protein Donor) |
O12 | OG | SER- 68 | 2.75 | 172.08 | H-Bond (Protein Donor) |
CB1 | CE1 | PHE- 108 | 3.74 | 0 | Hydrophobic |
CG1 | CZ | PHE- 108 | 4.29 | 0 | Hydrophobic |
SG2 | CZ | PHE- 108 | 3.74 | 0 | Hydrophobic |
OE1 | NH2 | ARG- 112 | 2.89 | 120.31 | H-Bond (Protein Donor) |
O32 | NH1 | ARG- 112 | 3.38 | 147.1 | H-Bond (Protein Donor) |
O32 | NH2 | ARG- 112 | 3.26 | 154.43 | H-Bond (Protein Donor) |
O32 | CZ | ARG- 112 | 3.78 | 0 | Ionic (Protein Cationic) |
C5S | CD1 | LEU- 119 | 3.91 | 0 | Hydrophobic |
C5S | CD1 | LEU- 207 | 3.57 | 0 | Hydrophobic |