2.450 Å
X-ray
2009-09-11
Name: | NAD(P)H dehydrogenase [quinone] 1 |
---|---|
ID: | NQO1_HUMAN |
AC: | P15559 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 1.6.5.2 |
Chain Name: | Percentage of Residues within binding site |
---|---|
D | 8 % |
E | 48 % |
G | 44 % |
B-Factor: | 67.230 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | FAD |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.289 | 1336.500 |
% Hydrophobic | % Polar |
---|---|
55.30 | 44.70 |
According to VolSite |
HET Code: | CC2 |
---|---|
Formula: | C22H17O3 |
Molecular weight: | 329.369 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 65.73 % |
Polar Surface area: | 49.36 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 0 |
Rings: | 4 |
Aromatic rings: | 3 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
35.1488 | -55.634 | 21.5195 |
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 |
C11 | CE3 | TRP- 105 | 3.33 | 0 | Hydrophobic |
C12 | CE2 | TRP- 105 | 3.81 | 0 | Hydrophobic |
C11 | CE2 | PHE- 106 | 3.72 | 0 | Hydrophobic |
C12 | CZ | TYR- 126 | 3.81 | 0 | Hydrophobic |
C13 | CE1 | TYR- 128 | 4.18 | 0 | Hydrophobic |
C17 | CB | TYR- 128 | 4.24 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 128 | 3.88 | 0 | Aromatic Face/Face |
C18 | CE | MET- 131 | 3.55 | 0 | Hydrophobic |
C19 | CE | MET- 154 | 3.81 | 0 | Hydrophobic |
O2 | NE2 | HIS- 161 | 3.14 | 134.5 | H-Bond (Protein Donor) |
O7 | NE2 | HIS- 161 | 3.18 | 161.42 | H-Bond (Protein Donor) |
C11 | CE2 | PHE- 178 | 3.64 | 0 | Hydrophobic |
C12 | C6 | FAD- 601 | 3.5 | 0 | Hydrophobic |