1.390 Å
X-ray
2013-05-15
Name: | Ketol-acid reductoisomerase (NADP(+)) |
---|---|
ID: | ILVC_SLAES |
AC: | D0WGK0 |
Organism: | Slackia exigua |
Reign: | Bacteria |
TaxID: | 649764 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 87 % |
B | 13 % |
B-Factor: | 13.310 |
---|---|
Number of residues: | 59 |
Including | |
Standard Amino Acids: | 52 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 5 |
Cofactors: | |
Metals: | MG MG |
Ligandability | Volume (Å3) |
---|---|
0.816 | 661.500 |
% Hydrophobic | % Polar |
---|---|
46.43 | 53.57 |
According to VolSite |
HET Code: | NAP |
---|---|
Formula: | C21H25N7O17P3 |
Molecular weight: | 740.381 g/mol |
DrugBank ID: | DB03461 |
Buried Surface Area: | 58.27 % |
Polar Surface area: | 405.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 21 |
H-Bond Donors: | 5 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 4 |
Cationic atoms: | 1 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
-12.2279 | 1.89773 | -14.9665 |
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 | N | TYR- 35 | 2.87 | 165.91 | H-Bond (Protein Donor) |
O1A | N | SER- 37 | 3 | 160.48 | H-Bond (Protein Donor) |
O1N | N | GLN- 38 | 2.9 | 168.81 | H-Bond (Protein Donor) |
O7N | NE2 | GLN- 38 | 3.06 | 171.72 | H-Bond (Protein Donor) |
C3N | CG | GLN- 38 | 3.4 | 0 | Hydrophobic |
O2B | NH2 | ARG- 58 | 3.14 | 146.5 | H-Bond (Protein Donor) |
O1X | NH2 | ARG- 58 | 3.32 | 140.66 | H-Bond (Protein Donor) |
DuAr | CZ | ARG- 58 | 3.49 | 178.85 | Pi/Cation |
O1X | OG | SER- 61 | 2.68 | 166.93 | H-Bond (Protein Donor) |
O2X | OG | SER- 63 | 2.5 | 158.23 | H-Bond (Protein Donor) |
C4D | CD2 | LEU- 90 | 3.85 | 0 | Hydrophobic |
C1B | CG1 | VAL- 91 | 3.84 | 0 | Hydrophobic |
O3D | OD1 | ASP- 93 | 2.65 | 161.13 | H-Bond (Ligand Donor) |
O2D | OD2 | ASP- 93 | 2.7 | 163.2 | H-Bond (Ligand Donor) |
O3D | NE2 | GLN- 96 | 3.11 | 137.07 | H-Bond (Protein Donor) |
C2D | CB | HIS- 118 | 4.17 | 0 | Hydrophobic |
O7N | N | GLY- 144 | 2.86 | 135.27 | H-Bond (Protein Donor) |
N7N | O | SER- 260 | 2.9 | 164.29 | H-Bond (Ligand Donor) |
C2D | CB | SER- 262 | 4.06 | 0 | Hydrophobic |
O3D | O | HOH- 501 | 2.8 | 179.98 | H-Bond (Protein Donor) |
O1N | O | HOH- 507 | 2.74 | 161.65 | H-Bond (Protein Donor) |
O1X | O | HOH- 531 | 2.79 | 179.95 | H-Bond (Protein Donor) |