2.200 Å
X-ray
2006-12-15
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 | 93 % |
B | 7 % |
B-Factor: | 22.437 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.581 | 320.625 |
% Hydrophobic | % Polar |
---|---|
58.95 | 41.05 |
According to VolSite |
HET Code: | GTB |
---|---|
Formula: | C17H21N4O8S |
Molecular weight: | 441.436 g/mol |
DrugBank ID: | DB03686 |
Buried Surface Area: | 57.72 % |
Polar Surface area: | 237.22 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 9 |
H-Bond Donors: | 3 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 3 |
Cationic atoms: | 2 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
25.435 | 14.1926 | -21.5844 |
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 | 3.75 | 0 | Hydrophobic |
CB2 | CE2 | PHE- 8 | 3.68 | 0 | Hydrophobic |
C3' | CB | PHE- 8 | 3.55 | 0 | Hydrophobic |
C3' | CG2 | VAL- 10 | 3.55 | 0 | Hydrophobic |
SG2 | CD | ARG- 13 | 4.42 | 0 | Hydrophobic |
CB1 | CD | ARG- 13 | 4.06 | 0 | Hydrophobic |
O31 | NE1 | TRP- 38 | 3.09 | 155 | H-Bond (Protein Donor) |
O31 | NZ | LYS- 44 | 3.06 | 171 | H-Bond (Protein Donor) |
O31 | NZ | LYS- 44 | 3.06 | 0 | Ionic (Protein Cationic) |
O32 | NZ | LYS- 44 | 3.84 | 0 | Ionic (Protein Cationic) |
CG1 | CB | GLN- 51 | 4 | 0 | Hydrophobic |
O32 | NE2 | GLN- 51 | 2.87 | 156.9 | H-Bond (Protein Donor) |
N2 | O | LEU- 52 | 2.75 | 152.57 | H-Bond (Ligand Donor) |
O2 | N | LEU- 52 | 2.81 | 169.47 | H-Bond (Protein Donor) |
N1 | OE1 | GLN- 64 | 2.71 | 126.3 | H-Bond (Ligand Donor) |
O11 | N | SER- 65 | 2.82 | 168.83 | H-Bond (Protein Donor) |
O12 | OG | SER- 65 | 2.68 | 146.29 | H-Bond (Protein Donor) |
O12 | N | SER- 65 | 3.35 | 135.57 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 98 | 3.71 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 98 | 3.19 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 98 | 3.19 | 164.07 | H-Bond (Ligand Donor) |
C' | CE2 | TYR- 108 | 4.36 | 0 | Hydrophobic |
O11 | O | HOH- 304 | 2.75 | 143.66 | H-Bond (Protein Donor) |