2.000 Å
X-ray
2011-05-12
Name: | NADPH-dependent 7-cyano-7-deazaguanine reductase |
---|---|
ID: | QUEF_VIBCH |
AC: | Q9KTK0 |
Organism: | Vibrio cholerae serotype O1 |
Reign: | Bacteria |
TaxID: | 243277 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
D | 100 % |
B-Factor: | 40.235 |
---|---|
Number of residues: | 17 |
Including | |
Standard Amino Acids: | 16 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.254 | 340.875 |
% Hydrophobic | % Polar |
---|---|
49.50 | 50.50 |
According to VolSite |
HET Code: | PRF |
---|---|
Formula: | C7H10N5O |
Molecular weight: | 180.187 g/mol |
DrugBank ID: | DB03304 |
Buried Surface Area: | 67.92 % |
Polar Surface area: | 110.91 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 4 |
Rings: | 2 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
-21.0258 | -27.878 | 0.763154 |
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 |
N2 | O | ILE- 93 | 2.69 | 155.22 | H-Bond (Ligand Donor) |
N9 | OE2 | GLU- 94 | 2.77 | 172.43 | H-Bond (Ligand Donor) |
N3 | N | SER- 95 | 2.79 | 145.82 | H-Bond (Protein Donor) |
N11 | OD2 | ASP- 201 | 2.78 | 147.61 | H-Bond (Ligand Donor) |
N11 | OD2 | ASP- 201 | 2.78 | 0 | Ionic (Ligand Cationic) |
DuAr | DuAr | PHE- 232 | 3.78 | 0 | Aromatic Face/Face |
O6 | N | HIS- 233 | 2.79 | 161.14 | H-Bond (Protein Donor) |
N1 | OE1 | GLU- 234 | 2.88 | 165.08 | H-Bond (Ligand Donor) |
N2 | OE2 | GLU- 234 | 2.75 | 173.14 | H-Bond (Ligand Donor) |