2.500 Å
X-ray
1997-01-20
Min | Mean | Median | Standard Deviation | Max | Count | |
---|---|---|---|---|---|---|
pChEMBL: | 5.000 | 5.000 | 5.000 | 0.000 | 5.000 | 1 |
Name: | Glutathione S-transferase P |
---|---|
ID: | GSTP1_HUMAN |
AC: | P09211 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.5.1.18 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 93 % |
B | 7 % |
B-Factor: | 27.353 |
---|---|
Number of residues: | 29 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.112 | 766.125 |
% Hydrophobic | % Polar |
---|---|
18.94 | 81.06 |
According to VolSite |
HET Code: | GTX |
---|---|
Formula: | C16H28N3O6S |
Molecular weight: | 390.475 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 50.7 % |
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 |
---|---|---|
10.4358 | 6.78054 | 27.439 |
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 | 4.17 | 0 | Hydrophobic |
C1S | CZ | TYR- 7 | 4.2 | 0 | Hydrophobic |
SG2 | CE2 | PHE- 8 | 3.35 | 0 | Hydrophobic |
C1S | CD2 | PHE- 8 | 4.28 | 0 | Hydrophobic |
C3S | CD2 | PHE- 8 | 3.89 | 0 | Hydrophobic |
C3S | CG2 | VAL- 10 | 4.42 | 0 | Hydrophobic |
C5S | CG1 | VAL- 10 | 4.24 | 0 | Hydrophobic |
O12 | CZ | ARG- 13 | 3.7 | 0 | Ionic (Protein Cationic) |
CG1 | CD | ARG- 13 | 3.96 | 0 | Hydrophobic |
C6S | CG2 | VAL- 35 | 3.74 | 0 | Hydrophobic |
O31 | NE1 | TRP- 38 | 2.94 | 164.35 | H-Bond (Protein Donor) |
O31 | NZ | LYS- 44 | 3.73 | 0 | Ionic (Protein Cationic) |
O32 | NZ | LYS- 44 | 3.97 | 0 | Ionic (Protein Cationic) |
CG1 | CB | GLN- 51 | 4.47 | 0 | Hydrophobic |
O32 | NE2 | GLN- 51 | 3.05 | 162.61 | H-Bond (Protein Donor) |
N2 | O | LEU- 52 | 3.01 | 157.13 | H-Bond (Ligand Donor) |
O2 | N | LEU- 52 | 3.17 | 169.79 | H-Bond (Protein Donor) |
N1 | OE1 | GLN- 64 | 2.63 | 154.44 | H-Bond (Ligand Donor) |
O11 | N | SER- 65 | 2.85 | 161.23 | H-Bond (Protein Donor) |
O12 | OG | SER- 65 | 2.76 | 157.94 | H-Bond (Protein Donor) |
O12 | N | SER- 65 | 3.46 | 142.97 | H-Bond (Protein Donor) |
N1 | OD2 | ASP- 98 | 2.97 | 142.99 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 98 | 2.97 | 0 | Ionic (Ligand Cationic) |
N1 | OD1 | ASP- 98 | 3.69 | 0 | Ionic (Ligand Cationic) |
C2S | CZ | PHE- 108 | 4.3 | 0 | Hydrophobic |
O11 | O | HOH- 221 | 2.96 | 179.96 | H-Bond (Protein Donor) |