2.100 Å
X-ray
1999-04-15
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 | 72 % |
B | 28 % |
B-Factor: | 24.562 |
---|---|
Number of residues: | 52 |
Including | |
Standard Amino Acids: | 50 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.181 | 1242.000 |
% Hydrophobic | % Polar |
---|---|
44.02 | 55.98 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 61.57 % |
Polar Surface area: | 381.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 7 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
39.6688 | 6.70609 | 31.5315 |
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 |
O1P | NE2 | HIS- 11 | 2.64 | 150.32 | H-Bond (Protein Donor) |
O2A | N | PHE- 17 | 2.77 | 168.89 | H-Bond (Protein Donor) |
C5B | CB | PHE- 17 | 3.31 | 0 | Hydrophobic |
O2P | N | ASN- 18 | 3.05 | 125.6 | H-Bond (Protein Donor) |
O2P | ND2 | ASN- 18 | 2.78 | 173.94 | H-Bond (Protein Donor) |
N7A | OG | SER- 20 | 2.56 | 156.86 | H-Bond (Protein Donor) |
N6A | OG | SER- 20 | 3.41 | 151.49 | H-Bond (Ligand Donor) |
O1A | ND2 | ASN- 66 | 3.28 | 127.87 | H-Bond (Protein Donor) |
C8M | CD2 | TYR- 67 | 3.62 | 0 | Hydrophobic |
C2' | CB | PRO- 102 | 4.44 | 0 | Hydrophobic |
C4' | CB | PRO- 102 | 3.79 | 0 | Hydrophobic |
O2' | O | LEU- 103 | 2.67 | 165.69 | H-Bond (Ligand Donor) |
C7M | CD2 | TYR- 104 | 3.78 | 0 | Hydrophobic |
C8M | CZ | TYR- 104 | 3.75 | 0 | Hydrophobic |
C6 | CB | TYR- 104 | 4.05 | 0 | Hydrophobic |
N5 | N | TRP- 105 | 2.79 | 168.83 | H-Bond (Protein Donor) |
O4 | N | PHE- 106 | 2.8 | 159.02 | H-Bond (Protein Donor) |
C7M | CB | ASP- 117 | 4.06 | 0 | Hydrophobic |
O4' | OG1 | THR- 147 | 2.72 | 177.14 | H-Bond (Protein Donor) |
N1 | N | GLY- 149 | 3.14 | 136.76 | H-Bond (Protein Donor) |
O2 | N | GLY- 149 | 2.86 | 130.97 | H-Bond (Protein Donor) |
O2 | N | GLY- 150 | 2.75 | 154.87 | H-Bond (Protein Donor) |
O2 | OH | TYR- 155 | 2.79 | 172.09 | H-Bond (Protein Donor) |
N3 | OH | TYR- 155 | 3.01 | 137.15 | H-Bond (Ligand Donor) |
C5B | CB | PRO- 192 | 4.19 | 0 | Hydrophobic |
C5' | CG | PRO- 192 | 3.95 | 0 | Hydrophobic |
C5B | CG | GLU- 193 | 4.33 | 0 | Hydrophobic |
C5' | CG | GLU- 193 | 3.69 | 0 | Hydrophobic |
O3' | OE1 | GLU- 193 | 2.61 | 137.85 | H-Bond (Ligand Donor) |
C4B | CD | ARG- 200 | 3.8 | 0 | Hydrophobic |
C1B | CD | ARG- 200 | 4.02 | 0 | Hydrophobic |