1.780 Å
X-ray
2009-04-14
Name: | Putative NADH-flavin reductase |
---|---|
ID: | Q03B84_LACC3 |
AC: | Q03B84 |
Organism: | Lactobacillus casei |
Reign: | Bacteria |
TaxID: | 321967 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 14.536 |
---|---|
Number of residues: | 48 |
Including | |
Standard Amino Acids: | 44 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 4 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.785 | 671.625 |
% Hydrophobic | % Polar |
---|---|
41.71 | 58.29 |
According to VolSite |
HET Code: | NDP |
---|---|
Formula: | C21H26N7O17P3 |
Molecular weight: | 741.389 g/mol |
DrugBank ID: | DB02338 |
Buried Surface Area: | 56.68 % |
Polar Surface area: | 404.9 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 5 |
Rings: | 5 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
20.7009 | 46.0531 | 9.23269 |
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 |
O3B | OG1 | THR- 9 | 3.09 | 160.5 | H-Bond (Ligand Donor) |
O1X | OG1 | THR- 9 | 2.57 | 148.45 | H-Bond (Protein Donor) |
O2A | N | ARG- 11 | 2.78 | 165.15 | H-Bond (Protein Donor) |
O2N | NH1 | ARG- 11 | 2.82 | 146.77 | H-Bond (Protein Donor) |
O2N | CZ | ARG- 11 | 3.94 | 0 | Ionic (Protein Cationic) |
O1N | N | ALA- 12 | 2.71 | 163.81 | H-Bond (Protein Donor) |
C5D | CB | ALA- 12 | 3.9 | 0 | Hydrophobic |
O2B | NE | ARG- 32 | 3.49 | 124.66 | H-Bond (Protein Donor) |
O2X | NE | ARG- 32 | 2.98 | 170.52 | H-Bond (Protein Donor) |
O3X | NH2 | ARG- 32 | 2.86 | 175.08 | H-Bond (Protein Donor) |
O2X | CZ | ARG- 32 | 3.88 | 0 | Ionic (Protein Cationic) |
O3X | CZ | ARG- 32 | 3.73 | 0 | Ionic (Protein Cationic) |
DuAr | CZ | ARG- 32 | 3.96 | 159.68 | Pi/Cation |
C1B | CD2 | LEU- 70 | 3.63 | 0 | Hydrophobic |
C5B | CB | SER- 71 | 3.77 | 0 | Hydrophobic |
C5D | CB | SER- 71 | 4.32 | 0 | Hydrophobic |
C3D | CB | SER- 71 | 3.69 | 0 | Hydrophobic |
O4B | N | SER- 71 | 3.35 | 157.32 | H-Bond (Protein Donor) |
O2D | OG | SER- 71 | 3.34 | 138.33 | H-Bond (Protein Donor) |
C5D | CD1 | ILE- 103 | 4.49 | 0 | Hydrophobic |
C4D | CG2 | ILE- 103 | 3.71 | 0 | Hydrophobic |
O7N | N | SER- 106 | 2.55 | 150.35 | H-Bond (Protein Donor) |
N7N | OG | SER- 106 | 2.78 | 152.07 | H-Bond (Ligand Donor) |
O3D | NE2 | GLN- 138 | 3.15 | 129.89 | H-Bond (Protein Donor) |
O2D | OE1 | GLN- 138 | 2.65 | 134.61 | H-Bond (Ligand Donor) |
C3N | CG | PRO- 158 | 4.13 | 0 | Hydrophobic |
N7N | O | GLU- 160 | 3.18 | 126.23 | H-Bond (Ligand Donor) |
C5D | CE2 | PHE- 162 | 4.34 | 0 | Hydrophobic |
C5N | CB | PHE- 162 | 3.65 | 0 | Hydrophobic |
O1N | O | HOH- 414 | 2.62 | 169.69 | H-Bond (Protein Donor) |
O2X | O | HOH- 447 | 2.72 | 179.94 | H-Bond (Protein Donor) |