1.700 Å
X-ray
2011-11-25
Name: | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase |
---|---|
ID: | ISPH_ECOLI |
AC: | P62623 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 15.366 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.882 | 266.625 |
% Hydrophobic | % Polar |
---|---|
51.90 | 48.10 |
According to VolSite |
HET Code: | 0CJ |
---|---|
Formula: | C5H9O8P2 |
Molecular weight: | 259.068 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 80.51 % |
Polar Surface area: | 158.47 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 8 |
H-Bond Donors: | 0 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
-38.4052 | -0.365067 | 15.8377 |
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 |
C28 | CG2 | VAL- 15 | 3.32 | 0 | Hydrophobic |
O15 | N | HIS- 41 | 2.76 | 176.29 | H-Bond (Protein Donor) |
O19 | ND1 | HIS- 41 | 2.83 | 163.12 | H-Bond (Protein Donor) |
C27 | CB | ALA- 73 | 4.26 | 0 | Hydrophobic |
O15 | NE2 | HIS- 74 | 2.91 | 151.68 | H-Bond (Protein Donor) |
O16 | NE2 | HIS- 74 | 3.3 | 123.98 | H-Bond (Protein Donor) |
C22 | CB | CYS- 96 | 4.45 | 0 | Hydrophobic |
C22 | CG2 | VAL- 99 | 3.42 | 0 | Hydrophobic |
O19 | NE2 | HIS- 124 | 2.93 | 167.14 | H-Bond (Protein Donor) |
C30 | CG2 | THR- 168 | 3.56 | 0 | Hydrophobic |
O18 | OG1 | THR- 168 | 2.84 | 158.92 | H-Bond (Protein Donor) |
O14 | OG | SER- 225 | 2.64 | 145.14 | H-Bond (Protein Donor) |
O19 | N | SER- 226 | 2.63 | 156.7 | H-Bond (Protein Donor) |
O20 | N | ASN- 227 | 2.72 | 167.26 | H-Bond (Protein Donor) |
O20 | ND2 | ASN- 227 | 2.83 | 154.78 | H-Bond (Protein Donor) |
C28 | CB | SER- 269 | 4.3 | 0 | Hydrophobic |
O14 | OG | SER- 269 | 2.72 | 156.93 | H-Bond (Protein Donor) |