1.700 Å
X-ray
2005-01-19
Name: | Oxygen-insensitive NAD(P)H nitroreductase |
---|---|
ID: | NFSB_ECOLI |
AC: | P38489 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 39 % |
B | 61 % |
B-Factor: | 18.613 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 38 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.371 | 1012.500 |
% Hydrophobic | % Polar |
---|---|
31.33 | 68.67 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 68.96 % |
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 |
---|---|---|
32.6739 | 10.3753 | 19.5574 |
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 | NH1 | ARG- 10 | 3.36 | 138.41 | H-Bond (Protein Donor) |
O2P | NH2 | ARG- 10 | 2.96 | 162.95 | H-Bond (Protein Donor) |
O3P | NH1 | ARG- 10 | 2.98 | 145.59 | H-Bond (Protein Donor) |
O2P | CZ | ARG- 10 | 3.61 | 0 | Ionic (Protein Cationic) |
O3P | CZ | ARG- 10 | 3.99 | 0 | Ionic (Protein Cationic) |
C1' | CB | SER- 12 | 3.8 | 0 | Hydrophobic |
C3' | CB | SER- 12 | 4.25 | 0 | Hydrophobic |
O1P | N | SER- 12 | 2.91 | 157.81 | H-Bond (Protein Donor) |
O2P | OG | SER- 12 | 2.65 | 159.1 | H-Bond (Protein Donor) |
O2 | NZ | LYS- 14 | 2.68 | 157.34 | H-Bond (Protein Donor) |
C8M | CB | PRO- 38 | 4.3 | 0 | Hydrophobic |
C7 | CB | SER- 40 | 3.92 | 0 | Hydrophobic |
C4' | CB | ASN- 42 | 3.7 | 0 | Hydrophobic |
N3 | OD1 | ASN- 71 | 3.37 | 147.75 | H-Bond (Ligand Donor) |
O4 | ND2 | ASN- 71 | 3.45 | 130.26 | H-Bond (Protein Donor) |
C7M | CE2 | TYR- 144 | 3.8 | 0 | Hydrophobic |
C7M | CD1 | LEU- 145 | 4.2 | 0 | Hydrophobic |
C8M | CD1 | LEU- 145 | 3.78 | 0 | Hydrophobic |
C1' | CG | PRO- 163 | 4.25 | 0 | Hydrophobic |
C7 | CB | PRO- 163 | 3.98 | 0 | Hydrophobic |
C8 | CG | PRO- 163 | 3.55 | 0 | Hydrophobic |
C9 | CG | PRO- 163 | 3.27 | 0 | Hydrophobic |
O4 | N | GLU- 165 | 3.41 | 121.08 | H-Bond (Protein Donor) |
N5 | N | GLU- 165 | 3.1 | 166.86 | H-Bond (Protein Donor) |
C7M | CG | GLU- 165 | 3.65 | 0 | Hydrophobic |
O4 | N | GLY- 166 | 3 | 144.91 | H-Bond (Protein Donor) |
O1P | NZ | LYS- 205 | 3.25 | 0 | Ionic (Protein Cationic) |
O3P | NZ | LYS- 205 | 2.64 | 0 | Ionic (Protein Cationic) |
O3P | NZ | LYS- 205 | 2.64 | 157.62 | H-Bond (Protein Donor) |
O3P | CZ | ARG- 207 | 3.65 | 0 | Ionic (Protein Cationic) |
O3P | NH2 | ARG- 207 | 2.78 | 178.39 | H-Bond (Protein Donor) |