2.000 Å
X-ray
2009-04-03
Name: | Dihydroorotate dehydrogenase (fumarate) |
---|---|
ID: | Q4QEW7_LEIMA |
AC: | Q4QEW7 |
Organism: | Leishmania major |
Reign: | Eukaryota |
TaxID: | 5664 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 13.761 |
---|---|
Number of residues: | 52 |
Including | |
Standard Amino Acids: | 47 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 5 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.754 | 847.125 |
% Hydrophobic | % Polar |
---|---|
31.87 | 68.13 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 73.55 % |
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 |
---|---|---|
51.1396 | -17.199 | -14.333 |
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 |
C2' | CB | ALA- 19 | 3.75 | 0 | Hydrophobic |
O2' | O | ALA- 20 | 2.85 | 159.43 | H-Bond (Ligand Donor) |
C7 | CG2 | VAL- 22 | 4.22 | 0 | Hydrophobic |
C8 | CG2 | VAL- 22 | 3.97 | 0 | Hydrophobic |
O4 | NZ | LYS- 44 | 2.76 | 153.73 | H-Bond (Protein Donor) |
N5 | NZ | LYS- 44 | 3.19 | 128.87 | H-Bond (Protein Donor) |
N3 | OG | SER- 45 | 2.67 | 157.64 | H-Bond (Ligand Donor) |
C7M | CD2 | TYR- 59 | 3.91 | 0 | Hydrophobic |
C8M | CE2 | TYR- 59 | 3.88 | 0 | Hydrophobic |
C7M | CG | MET- 70 | 3.71 | 0 | Hydrophobic |
O2 | NZ | LYS- 165 | 3.04 | 170.89 | H-Bond (Protein Donor) |
O2' | NZ | LYS- 165 | 2.91 | 145.11 | H-Bond (Protein Donor) |
O3' | NZ | LYS- 165 | 3.23 | 135.77 | H-Bond (Protein Donor) |
O3' | O | ILE- 194 | 2.86 | 139.58 | H-Bond (Ligand Donor) |
O1P | N | GLY- 223 | 2.65 | 161.87 | H-Bond (Protein Donor) |
C3' | SG | CYS- 249 | 3.48 | 0 | Hydrophobic |
O1P | N | GLY- 251 | 2.77 | 162.96 | H-Bond (Protein Donor) |
O3P | N | GLY- 272 | 2.83 | 143.34 | H-Bond (Protein Donor) |
O2P | N | THR- 273 | 2.74 | 162 | H-Bond (Protein Donor) |
O2P | OG1 | THR- 273 | 2.73 | 163.04 | H-Bond (Protein Donor) |
O3P | N | THR- 273 | 3.39 | 132.13 | H-Bond (Protein Donor) |
O3P | O | HOH- 351 | 2.62 | 154.89 | H-Bond (Protein Donor) |
O3P | O | HOH- 359 | 2.76 | 177.42 | H-Bond (Protein Donor) |