1.950 Å
X-ray
2010-09-06
Name: | Transcriptional repressor, TetR family |
---|---|
ID: | Q5SM42_THET8 |
AC: | Q5SM42 |
Organism: | Thermus thermophilus |
Reign: | Bacteria |
TaxID: | 300852 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 23 % |
B | 77 % |
B-Factor: | 21.274 |
---|---|
Number of residues: | 48 |
Including | |
Standard Amino Acids: | 48 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.164 | 560.250 |
% Hydrophobic | % Polar |
---|---|
69.28 | 30.72 |
According to VolSite |
HET Code: | DCC |
---|---|
Formula: | C33H54N7O17P3S |
Molecular weight: | 945.805 g/mol |
DrugBank ID: | DB03264 |
Buried Surface Area: | 45.27 % |
Polar Surface area: | 429.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 30 |
X | Y | Z |
---|---|---|
38.6973 | 38.7697 | 17.5604 |
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 |
C12 | CB | LEU- 64 | 4.22 | 0 | Hydrophobic |
C10 | CD2 | LEU- 93 | 4.23 | 0 | Hydrophobic |
C12 | CD2 | LEU- 93 | 3.93 | 0 | Hydrophobic |
C11 | CD2 | LEU- 104 | 4.2 | 0 | Hydrophobic |
C11 | CE | MET- 107 | 4.22 | 0 | Hydrophobic |
CA9 | CE | MET- 107 | 3.91 | 0 | Hydrophobic |
CA9 | CE1 | PHE- 108 | 4.27 | 0 | Hydrophobic |
CA2 | CD1 | LEU- 111 | 4.44 | 0 | Hydrophobic |
CA5 | CD1 | LEU- 111 | 3.56 | 0 | Hydrophobic |
S | CD2 | LEU- 112 | 4.32 | 0 | Hydrophobic |
OP2 | NE | ARG- 120 | 3.3 | 135.11 | H-Bond (Protein Donor) |
CP7 | CD2 | PHE- 123 | 3.82 | 0 | Hydrophobic |
CP9 | CE1 | PHE- 123 | 3.73 | 0 | Hydrophobic |
CA3 | CE1 | PHE- 123 | 3.52 | 0 | Hydrophobic |
CA7 | CB | LEU- 126 | 4.08 | 0 | Hydrophobic |
CA6 | CB | LEU- 128 | 4.23 | 0 | Hydrophobic |
CA8 | CB | LEU- 128 | 4.05 | 0 | Hydrophobic |
O32 | OG | SER- 150 | 2.85 | 150.27 | H-Bond (Protein Donor) |
O33 | NE | ARG- 153 | 3.17 | 164.41 | H-Bond (Protein Donor) |
CA9 | CE2 | TYR- 162 | 3.9 | 0 | Hydrophobic |
CA8 | CE2 | TYR- 162 | 3.68 | 0 | Hydrophobic |
S | CE2 | PHE- 163 | 3.76 | 0 | Hydrophobic |
CA2 | CG | PHE- 163 | 3.56 | 0 | Hydrophobic |
CA5 | CB | PHE- 163 | 4.03 | 0 | Hydrophobic |
S | CD2 | LEU- 164 | 3.97 | 0 | Hydrophobic |
CP8 | CD | ARG- 168 | 4.41 | 0 | Hydrophobic |
CP9 | CD | ARG- 168 | 3.87 | 0 | Hydrophobic |
CP4 | CG | ARG- 168 | 4.5 | 0 | Hydrophobic |
CP1 | CB | ARG- 168 | 4.48 | 0 | Hydrophobic |
OA1 | NH2 | ARG- 168 | 2.76 | 145.88 | H-Bond (Protein Donor) |
CP4 | CG | TYR- 172 | 3.44 | 0 | Hydrophobic |
CP8 | CG2 | THR- 173 | 3.7 | 0 | Hydrophobic |
O22 | NH1 | ARG- 176 | 2.97 | 138.64 | H-Bond (Protein Donor) |
O22 | NH2 | ARG- 176 | 2.82 | 146.04 | H-Bond (Protein Donor) |
O22 | CZ | ARG- 176 | 3.31 | 0 | Ionic (Protein Cationic) |
DuAr | CZ | ARG- 176 | 3.31 | 176.37 | Pi/Cation |