2.440 Å
X-ray
2011-08-20
Name: | Nucleoside permease |
---|---|
ID: | Q9KPL5_VIBCH |
AC: | Q9KPL5 |
Organism: | Vibrio cholerae serotype O1 |
Reign: | Bacteria |
TaxID: | 243277 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 46.536 |
---|---|
Number of residues: | 28 |
Including | |
Standard Amino Acids: | 26 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.859 | 347.625 |
% Hydrophobic | % Polar |
---|---|
59.22 | 40.78 |
According to VolSite |
HET Code: | URI |
---|---|
Formula: | C9H12N2O6 |
Molecular weight: | 244.201 g/mol |
DrugBank ID: | DB02745 |
Buried Surface Area: | 62.29 % |
Polar Surface area: | 119.33 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 4 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
51.3141 | -19.4992 | -8.47059 |
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 |
O2 | NE2 | GLN- 154 | 2.87 | 160.72 | H-Bond (Protein Donor) |
C5' | CB | ASN- 331 | 4.24 | 0 | Hydrophobic |
O3' | OE1 | GLU- 332 | 2.68 | 168.23 | H-Bond (Ligand Donor) |
O5' | OE2 | GLU- 332 | 2.67 | 168.54 | H-Bond (Ligand Donor) |
C5' | CB | PHE- 333 | 3.96 | 0 | Hydrophobic |
C2' | CG | PHE- 366 | 3.86 | 0 | Hydrophobic |
C3' | CD1 | PHE- 366 | 3.6 | 0 | Hydrophobic |
O3' | ND2 | ASN- 368 | 3.11 | 144.09 | H-Bond (Protein Donor) |
O2' | OG | SER- 371 | 2.69 | 160.33 | H-Bond (Ligand Donor) |
C1' | CD1 | ILE- 374 | 3.88 | 0 | Hydrophobic |
N3 | O | HOH- 426 | 2.84 | 177.31 | H-Bond (Ligand Donor) |