1.500 Å
X-ray
2006-06-23
Name: | Lipopolysaccharide core biosynthesis protein RfaG |
---|---|
ID: | RFAG_ECOLI |
AC: | P25740 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 2.4 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 8.075 |
---|---|
Number of residues: | 53 |
Including | |
Standard Amino Acids: | 47 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 6 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.221 | 874.125 |
% Hydrophobic | % Polar |
---|---|
32.82 | 67.18 |
According to VolSite |
HET Code: | U2F |
---|---|
Formula: | C15H21FN2O16P2 |
Molecular weight: | 566.277 g/mol |
DrugBank ID: | DB03488 |
Buried Surface Area: | 77.53 % |
Polar Surface area: | 296.59 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
H-Bond Donors: | 6 |
Rings: | 3 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
-5.63092 | 10.8896 | -19.0942 |
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 |
O1B | N | GLY- 15 | 2.75 | 168.49 | H-Bond (Protein Donor) |
C1' | CD | ARG- 18 | 3.69 | 0 | Hydrophobic |
C4' | CD | ARG- 18 | 3.98 | 0 | Hydrophobic |
O6 | OD2 | ASP- 19 | 2.74 | 159.43 | H-Bond (Ligand Donor) |
C6 | CE2 | PHE- 97 | 4.24 | 0 | Hydrophobic |
C6 | CB | ALA- 99 | 3.87 | 0 | Hydrophobic |
C4 | CD1 | LEU- 143 | 4.45 | 0 | Hydrophobic |
C6 | CD1 | LEU- 143 | 3.82 | 0 | Hydrophobic |
O2' | NH2 | ARG- 173 | 3.08 | 142.02 | H-Bond (Protein Donor) |
C2' | CG1 | VAL- 202 | 4.18 | 0 | Hydrophobic |
O2B | CZ | ARG- 208 | 3.83 | 0 | Ionic (Protein Cationic) |
O2B | NH2 | ARG- 208 | 2.78 | 157.67 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 209 | 2.82 | 152.13 | H-Bond (Protein Donor) |
O3A | NZ | LYS- 209 | 2.93 | 127.47 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 209 | 2.82 | 0 | Ionic (Protein Cationic) |
N3 | O | ARG- 261 | 2.83 | 173.19 | H-Bond (Ligand Donor) |
O7' | N | ARG- 261 | 2.98 | 165.35 | H-Bond (Protein Donor) |
O3 | OE2 | GLU- 281 | 2.67 | 155.4 | H-Bond (Ligand Donor) |
O3 | N | ALA- 283 | 2.96 | 166.11 | H-Bond (Protein Donor) |
C4 | CB | ALA- 283 | 4.16 | 0 | Hydrophobic |
O4 | N | GLY- 284 | 2.93 | 164.89 | H-Bond (Protein Donor) |
O1A | N | ILE- 285 | 2.79 | 158.88 | H-Bond (Protein Donor) |
C3' | CG2 | ILE- 285 | 4 | 0 | Hydrophobic |
C6 | CD1 | ILE- 285 | 4.13 | 0 | Hydrophobic |
O2A | N | VAL- 286 | 3.14 | 160.43 | H-Bond (Protein Donor) |
C5' | CG1 | VAL- 286 | 4.46 | 0 | Hydrophobic |
C2' | CG1 | VAL- 286 | 3.74 | 0 | Hydrophobic |
O3' | OE2 | GLU- 289 | 2.63 | 174.35 | H-Bond (Ligand Donor) |
O2' | OE2 | GLU- 289 | 3.09 | 131.14 | H-Bond (Ligand Donor) |
O2' | OE1 | GLU- 289 | 2.65 | 162.74 | H-Bond (Ligand Donor) |
O2A | O | HOH- 2583 | 2.73 | 138.17 | H-Bond (Protein Donor) |
O1B | O | HOH- 2584 | 2.78 | 175.61 | H-Bond (Protein Donor) |