1.200 Å
X-ray
2012-12-23
Name: | NAD(P)H dehydrogenase (quinone) |
---|---|
ID: | NQOR_ECOLI |
AC: | P0A8G6 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 79 % |
B | 21 % |
B-Factor: | 12.781 |
---|---|
Number of residues: | 42 |
Including | |
Standard Amino Acids: | 38 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.756 | 550.125 |
% Hydrophobic | % Polar |
---|---|
42.33 | 57.67 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 67.71 % |
Polar Surface area: | 217.05 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 12 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
-11.3223 | 15.2816 | -2.3139 |
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 |
O2P | OG | SER- 9 | 2.62 | 149.11 | H-Bond (Protein Donor) |
O3P | N | SME- 10 | 2.8 | 143.95 | H-Bond (Protein Donor) |
O1P | N | TYR- 11 | 3.04 | 129.42 | H-Bond (Protein Donor) |
O3P | N | TYR- 11 | 3.04 | 159.58 | H-Bond (Protein Donor) |
C5' | CB | HIS- 13 | 4.2 | 0 | Hydrophobic |
O1P | N | HIS- 13 | 2.87 | 164.85 | H-Bond (Protein Donor) |
O2P | N | ILE- 14 | 2.77 | 169.68 | H-Bond (Protein Donor) |
C4' | CB | PRO- 76 | 3.73 | 0 | Hydrophobic |
O2' | O | THR- 77 | 2.74 | 168.16 | H-Bond (Ligand Donor) |
C7 | CD | ARG- 78 | 3.51 | 0 | Hydrophobic |
C8 | CD | ARG- 78 | 3.53 | 0 | Hydrophobic |
C8 | CD | ARG- 78 | 3.53 | 0 | Hydrophobic |
N5 | N | PHE- 79 | 2.98 | 164.68 | H-Bond (Protein Donor) |
C7M | CE2 | PHE- 79 | 3.87 | 0 | Hydrophobic |
C7M | CB | ASP- 91 | 4.3 | 0 | Hydrophobic |
C4' | CB | SER- 112 | 4.37 | 0 | Hydrophobic |
O4' | OG | SER- 112 | 2.81 | 155.87 | H-Bond (Protein Donor) |
N1 | N | GLY- 114 | 3.02 | 159.69 | H-Bond (Protein Donor) |
O2 | N | GLY- 114 | 3.13 | 123.13 | H-Bond (Protein Donor) |
O2 | N | THR- 115 | 2.89 | 173.02 | H-Bond (Protein Donor) |
O2 | N | GLY- 116 | 3.35 | 122.19 | H-Bond (Protein Donor) |
N3 | O | GLY- 117 | 2.71 | 154.65 | H-Bond (Ligand Donor) |
C3' | CB | ALA- 165 | 4.38 | 0 | Hydrophobic |
C5' | CB | ALA- 165 | 4.42 | 0 | Hydrophobic |
O3P | O | HOH- 2088 | 2.74 | 161.58 | H-Bond (Protein Donor) |
O2 | O | HOH- 2118 | 3.17 | 132.1 | H-Bond (Protein Donor) |