1.790 Å
X-ray
2010-10-28
Name: | dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase |
---|---|
ID: | TYLM1_STRFR |
AC: | P95748 |
Organism: | Streptomyces fradiae |
Reign: | Bacteria |
TaxID: | 1906 |
EC Number: | 2.1.1.235 |
Chain Name: | Percentage of Residues within binding site |
---|---|
D | 100 % |
B-Factor: | 13.865 |
---|---|
Number of residues: | 36 |
Including | |
Standard Amino Acids: | 34 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.944 | 1046.250 |
% Hydrophobic | % Polar |
---|---|
49.03 | 50.97 |
According to VolSite |
HET Code: | T3Q |
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Formula: | C16H26N3O14P2 |
Molecular weight: | 546.337 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 66.66 % |
Polar Surface area: | 283.77 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
-44.583 | 2.8524 | 7.8214 |
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 |
O4Q | OH | TYR- 14 | 2.55 | 173.01 | H-Bond (Ligand Donor) |
C4Q | CZ | TYR- 14 | 4.49 | 0 | Hydrophobic |
O1A | NZ | LYS- 29 | 2.93 | 160.44 | H-Bond (Protein Donor) |
O1A | NZ | LYS- 29 | 2.93 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 29 | 2.9 | 0 | Ionic (Protein Cationic) |
N3Q | O | PHE- 118 | 2.85 | 150.91 | H-Bond (Ligand Donor) |
C2Q | CZ | PHE- 118 | 4.34 | 0 | Hydrophobic |
C4' | CH2 | TRP- 152 | 3.82 | 0 | Hydrophobic |
C2Q | CZ3 | TRP- 152 | 3.84 | 0 | Hydrophobic |
C5M | CZ2 | TRP- 153 | 4.29 | 0 | Hydrophobic |
C1' | CE2 | TRP- 153 | 3.8 | 0 | Hydrophobic |
O4' | NE1 | TRP- 153 | 2.85 | 138.27 | H-Bond (Protein Donor) |
C2' | CE1 | PHE- 158 | 4.16 | 0 | Hydrophobic |
O2 | N | THR- 159 | 2.97 | 159.38 | H-Bond (Protein Donor) |
C5M | CZ | TYR- 162 | 3.86 | 0 | Hydrophobic |
C5' | CE1 | TYR- 162 | 3.99 | 0 | Hydrophobic |
C2' | CD1 | TYR- 162 | 3.5 | 0 | Hydrophobic |
O2A | NH2 | ARG- 177 | 2.79 | 143.74 | H-Bond (Protein Donor) |
O2A | NH1 | ARG- 177 | 2.8 | 142.72 | H-Bond (Protein Donor) |
O2A | CZ | ARG- 177 | 3.22 | 0 | Ionic (Protein Cationic) |
O2A | OG | SER- 179 | 2.56 | 170.39 | H-Bond (Protein Donor) |
O3' | OG | SER- 181 | 2.65 | 164.47 | H-Bond (Protein Donor) |
C3' | CB | SER- 181 | 3.92 | 0 | Hydrophobic |
C6Q | CG2 | ILE- 190 | 4.11 | 0 | Hydrophobic |
C3' | CD1 | ILE- 190 | 4.18 | 0 | Hydrophobic |
C4Q | CD1 | ILE- 212 | 4.48 | 0 | Hydrophobic |
C6Q | CD1 | ILE- 212 | 4.46 | 0 | Hydrophobic |
O1B | CZ | ARG- 241 | 3.77 | 0 | Ionic (Protein Cationic) |
O1B | NH2 | ARG- 241 | 2.73 | 151.13 | H-Bond (Protein Donor) |
O2Q | NH1 | ARG- 241 | 2.85 | 170.04 | H-Bond (Protein Donor) |