1.890 Å
X-ray
2007-05-14
Name: | Bifunctional protein GlmU |
---|---|
ID: | GLMU_HAEIN |
AC: | P43889 |
Organism: | Haemophilus influenzae |
Reign: | Bacteria |
TaxID: | 71421 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 25.753 |
---|---|
Number of residues: | 50 |
Including | |
Standard Amino Acids: | 45 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 5 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.478 | 452.250 |
% Hydrophobic | % Polar |
---|---|
41.04 | 58.96 |
According to VolSite |
HET Code: | UD1 |
---|---|
Formula: | C17H25N3O17P2 |
Molecular weight: | 605.338 g/mol |
DrugBank ID: | DB03397 |
Buried Surface Area: | 58.29 % |
Polar Surface area: | 325.69 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 7 |
Rings: | 3 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 10 |
X | Y | Z |
---|---|---|
68.4327 | 4.83023 | 78.7729 |
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 |
C1B | CB | LEU- 11 | 4.12 | 0 | Hydrophobic |
O2 | N | ALA- 13 | 3.07 | 151.19 | H-Bond (Protein Donor) |
N3 | OE1 | GLN- 76 | 2.87 | 167.82 | H-Bond (Ligand Donor) |
O4 | NE2 | GLN- 76 | 2.96 | 140.62 | H-Bond (Protein Donor) |
O4 | N | GLY- 81 | 2.99 | 153.31 | H-Bond (Protein Donor) |
O7' | OG1 | THR- 82 | 2.76 | 164.53 | H-Bond (Protein Donor) |
C5B | CG2 | THR- 82 | 4.02 | 0 | Hydrophobic |
C4B | CD1 | TYR- 103 | 3.65 | 0 | Hydrophobic |
C5B | CE1 | TYR- 103 | 4.23 | 0 | Hydrophobic |
O3B | OD2 | ASP- 105 | 2.75 | 158.84 | H-Bond (Ligand Donor) |
C6' | CD2 | TYR- 139 | 4.21 | 0 | Hydrophobic |
O3' | N | GLY- 140 | 3.5 | 125.41 | H-Bond (Protein Donor) |
O4' | N | GLY- 140 | 2.86 | 150.18 | H-Bond (Protein Donor) |
C8' | CG | GLU- 154 | 4.1 | 0 | Hydrophobic |
N2' | OE2 | GLU- 154 | 2.8 | 166.85 | H-Bond (Ligand Donor) |
O3' | OE1 | GLU- 154 | 2.63 | 170.27 | H-Bond (Ligand Donor) |
O3' | ND2 | ASN- 169 | 2.89 | 166.8 | H-Bond (Protein Donor) |
O4' | O | ASN- 169 | 2.76 | 158.04 | H-Bond (Ligand Donor) |
C4' | CB | ASN- 169 | 4 | 0 | Hydrophobic |
C8' | CD1 | TYR- 197 | 3.5 | 0 | Hydrophobic |
C3' | CG2 | THR- 199 | 4.4 | 0 | Hydrophobic |
C8' | CG2 | THR- 199 | 4.07 | 0 | Hydrophobic |
O2B | O | HOH- 2089 | 3.08 | 179.97 | H-Bond (Protein Donor) |
O3B | O | HOH- 2282 | 2.66 | 140.49 | H-Bond (Protein Donor) |