2.330 Å
X-ray
2010-06-14
Name: | Ribosyldihydronicotinamide dehydrogenase [quinone] |
---|---|
ID: | NQO2_HUMAN |
AC: | P16083 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 56 % |
B | 44 % |
B-Factor: | 40.709 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | FAD |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.964 | 502.875 |
% Hydrophobic | % Polar |
---|---|
56.38 | 43.62 |
According to VolSite |
HET Code: | A2Z |
---|---|
Formula: | C12H11NO3 |
Molecular weight: | 217.221 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 65.27 % |
Polar Surface area: | 38.77 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 0 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 0 |
X | Y | Z |
---|---|---|
-3.71625 | -6.917 | -15.8821 |
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 |
C15 | CE3 | TRP- 105 | 4 | 0 | Hydrophobic |
C15 | CE1 | PHE- 106 | 3.89 | 0 | Hydrophobic |
C12 | CZ | PHE- 126 | 4.25 | 0 | Hydrophobic |
O3 | ND2 | ASN- 161 | 2.82 | 154.24 | H-Bond (Protein Donor) |
C15 | CD1 | PHE- 178 | 3.55 | 0 | Hydrophobic |
C12 | C1' | FAD- 232 | 3.57 | 0 | Hydrophobic |
C4 | C1' | FAD- 232 | 3.99 | 0 | Hydrophobic |