2.300 Å
X-ray
2003-06-24
Name: | HAT A1 |
---|---|
ID: | Q27198_TETTH |
AC: | Q27198 |
Organism: | Tetrahymena thermophila |
Reign: | Eukaryota |
TaxID: | 5911 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 85 % |
B | 15 % |
B-Factor: | 25.252 |
---|---|
Number of residues: | 35 |
Including | |
Standard Amino Acids: | 34 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.969 | 583.875 |
% Hydrophobic | % Polar |
---|---|
49.71 | 50.29 |
According to VolSite |
HET Code: | COA |
---|---|
Formula: | C21H32N7O16P3S |
Molecular weight: | 763.502 g/mol |
DrugBank ID: | DB01992 |
Buried Surface Area: | 52.35 % |
Polar Surface area: | 426.11 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 21 |
H-Bond Donors: | 6 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 18 |
X | Y | Z |
---|---|---|
45.7824 | 26.8294 | 7.56177 |
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 |
C6P | CB | GLN- 76 | 3.96 | 0 | Hydrophobic |
C6P | CD2 | LEU- 77 | 3.88 | 0 | Hydrophobic |
S1P | CD2 | LEU- 77 | 3.38 | 0 | Hydrophobic |
CEP | CG | LEU- 126 | 4.1 | 0 | Hydrophobic |
S1P | CB | LEU- 126 | 4.45 | 0 | Hydrophobic |
N4P | O | LEU- 126 | 2.79 | 148.28 | H-Bond (Ligand Donor) |
C6P | CB | ALA- 127 | 3.97 | 0 | Hydrophobic |
CEP | CG2 | VAL- 128 | 3.84 | 0 | Hydrophobic |
O9P | N | VAL- 128 | 2.76 | 159.26 | H-Bond (Protein Donor) |
CAP | CG | GLN- 133 | 4.18 | 0 | Hydrophobic |
O9P | NE2 | GLN- 133 | 3.17 | 142.86 | H-Bond (Protein Donor) |
C2B | CG1 | VAL- 134 | 4.11 | 0 | Hydrophobic |
O4A | N | VAL- 134 | 3.03 | 171.82 | H-Bond (Protein Donor) |
O1A | N | GLY- 136 | 2.94 | 137.54 | H-Bond (Protein Donor) |
O5A | N | GLY- 138 | 3.27 | 144.12 | H-Bond (Protein Donor) |
O2A | N | THR- 139 | 3.21 | 129.33 | H-Bond (Protein Donor) |
O2A | OG1 | THR- 139 | 2.95 | 162.35 | H-Bond (Protein Donor) |
CDP | CZ | PHE- 164 | 4.39 | 0 | Hydrophobic |
CDP | CD1 | TYR- 168 | 4.01 | 0 | Hydrophobic |
CEP | CZ | TYR- 168 | 4.49 | 0 | Hydrophobic |
CCP | CE1 | TYR- 168 | 3.66 | 0 | Hydrophobic |
C2P | CE1 | PHE- 169 | 4.44 | 0 | Hydrophobic |
C2P | CD | LYS- 314 | 3.72 | 0 | Hydrophobic |
S1P | CB | LYS- 314 | 3.26 | 0 | Hydrophobic |
S1P | NZ | LYS- 314 | 2.65 | 156.77 | Weak HBond PROT |
C2P | CG | PRO- 316 | 3.75 | 0 | Hydrophobic |