2.200 Å
X-ray
1994-05-04
Name: | Glutathione S-transferase P 1 |
---|---|
ID: | GSTP1_MOUSE |
AC: | P19157 |
Organism: | Mus musculus |
Reign: | Eukaryota |
TaxID: | 10090 |
EC Number: | 2.5.1.18 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 8 % |
B | 92 % |
B-Factor: | 13.498 |
---|---|
Number of residues: | 28 |
Including | |
Standard Amino Acids: | 26 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.382 | 540.000 |
% Hydrophobic | % Polar |
---|---|
43.75 | 56.25 |
According to VolSite |
HET Code: | GTX |
---|---|
Formula: | C16H28N3O6S |
Molecular weight: | 390.475 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 51.97 % |
Polar Surface area: | 191.4 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 3 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 15 |
X | Y | Z |
---|---|---|
58.2438 | 29.7319 | 9.4805 |
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 |
SG2 | CE1 | TYR- 7 | 3.78 | 0 | Hydrophobic |
CB2 | CE2 | PHE- 8 | 3.89 | 0 | Hydrophobic |
C5S | CG | PHE- 8 | 4.48 | 0 | Hydrophobic |
C3S | CD2 | PHE- 8 | 4.24 | 0 | Hydrophobic |
C2S | CG2 | VAL- 10 | 4 | 0 | Hydrophobic |
O11 | CZ | ARG- 13 | 3.89 | 0 | Ionic (Protein Cationic) |
CB1 | CD | ARG- 13 | 4 | 0 | Hydrophobic |
C5S | CD1 | ILE- 35 | 3.74 | 0 | Hydrophobic |
O31 | NE1 | TRP- 38 | 3.01 | 163.4 | H-Bond (Protein Donor) |
O31 | NZ | LYS- 44 | 2.91 | 152 | H-Bond (Protein Donor) |
O31 | NZ | LYS- 44 | 2.91 | 0 | Ionic (Protein Cationic) |
O32 | NZ | LYS- 44 | 3.49 | 0 | Ionic (Protein Cationic) |
CG1 | CB | GLN- 51 | 4.27 | 0 | Hydrophobic |
O32 | NE2 | GLN- 51 | 2.94 | 177.53 | H-Bond (Protein Donor) |
N2 | O | LEU- 52 | 3.02 | 157.34 | H-Bond (Ligand Donor) |
O2 | N | LEU- 52 | 2.94 | 167.02 | H-Bond (Protein Donor) |
N1 | OE1 | GLN- 64 | 2.8 | 126.84 | H-Bond (Ligand Donor) |
O11 | OG | SER- 65 | 2.81 | 159.58 | H-Bond (Protein Donor) |
O11 | N | SER- 65 | 3.36 | 150.06 | H-Bond (Protein Donor) |
O12 | N | SER- 65 | 2.91 | 152.83 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 98 | 3.71 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 98 | 3.14 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 98 | 3.14 | 159.6 | H-Bond (Ligand Donor) |
C4S | CE1 | TYR- 108 | 4.34 | 0 | Hydrophobic |
C2S | CZ | TYR- 108 | 4.35 | 0 | Hydrophobic |
O12 | O | HOH- 234 | 2.83 | 134.19 | H-Bond (Protein Donor) |