1.500 Å
X-ray
2004-09-21
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 | 33 % |
B | 67 % |
B-Factor: | 19.051 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 23 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | FAD |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.722 | 533.250 |
% Hydrophobic | % Polar |
---|---|
47.47 | 52.53 |
According to VolSite |
HET Code: | CB1 |
---|---|
Formula: | C9H8N4O5 |
Molecular weight: | 252.184 g/mol |
DrugBank ID: | DB04253 |
Buried Surface Area: | 54.93 % |
Polar Surface area: | 137.73 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 1 |
Rings: | 2 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 2 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
24.1266 | 14.8728 | 4.63722 |
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 |
C7 | CE2 | PHE- 126 | 3.98 | 0 | Hydrophobic |
C9 | CZ | PHE- 126 | 3.77 | 0 | Hydrophobic |
N | ND2 | ASN- 161 | 3.35 | 152.47 | H-Bond (Protein Donor) |
O1 | ND2 | ASN- 161 | 2.78 | 133.21 | H-Bond (Protein Donor) |
O2 | ND2 | ASN- 161 | 3.12 | 164.23 | H-Bond (Protein Donor) |
C | CZ | PHE- 178 | 3.48 | 0 | Hydrophobic |
C5 | C1' | FAD- 1233 | 4.5 | 0 | Hydrophobic |
C7 | C1' | FAD- 1233 | 4.18 | 0 | Hydrophobic |
C9 | C9A | FAD- 1233 | 3.25 | 0 | Hydrophobic |