1.500 Å
X-ray
2001-10-03
Min | Mean | Median | Standard Deviation | Max | Count | |
---|---|---|---|---|---|---|
pChEMBL: | 6.080 | 6.080 | 6.080 | 0.000 | 6.080 | 1 |
Name: | Glutathione S-transferase A1 |
---|---|
ID: | GSTA1_HUMAN |
AC: | P08263 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.5.1.18 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 88 % |
B | 12 % |
B-Factor: | 22.686 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 32 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 5 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.387 | 2089.125 |
% Hydrophobic | % Polar |
---|---|
41.52 | 58.48 |
According to VolSite |
HET Code: | GTX |
---|---|
Formula: | C16H28N3O6S |
Molecular weight: | 390.475 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 59.17 % |
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 |
---|---|---|
81.4767 | 27.7589 | 14.7395 |
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- 9 | 4.04 | 0 | Hydrophobic |
SG2 | CD | ARG- 15 | 3.82 | 0 | Hydrophobic |
C2S | CG | ARG- 15 | 4.39 | 0 | Hydrophobic |
CG1 | CD | ARG- 15 | 3.93 | 0 | Hydrophobic |
CG1 | CB | GLN- 54 | 4.27 | 0 | Hydrophobic |
O32 | NE2 | GLN- 54 | 3.09 | 166.35 | H-Bond (Protein Donor) |
N2 | O | VAL- 55 | 2.61 | 159.8 | H-Bond (Ligand Donor) |
O2 | N | VAL- 55 | 3.12 | 149.15 | H-Bond (Protein Donor) |
O11 | N | THR- 68 | 3.06 | 153.68 | H-Bond (Protein Donor) |
O11 | OG1 | THR- 68 | 3.27 | 128.95 | H-Bond (Protein Donor) |
O12 | OG1 | THR- 68 | 2.87 | 166.59 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 101 | 3.27 | 133.44 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 101 | 2.92 | 163.06 | H-Bond (Ligand Donor) |
N1 | OD1 | ASP- 101 | 3.27 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 101 | 2.92 | 0 | Ionic (Ligand Cationic) |
C4S | CD1 | LEU- 107 | 4.44 | 0 | Hydrophobic |
C6S | CG | PRO- 110 | 4.28 | 0 | Hydrophobic |
C6S | CG2 | VAL- 111 | 3.29 | 0 | Hydrophobic |
O31 | CZ | ARG- 131 | 3.61 | 0 | Ionic (Protein Cationic) |
O32 | CZ | ARG- 131 | 3.85 | 0 | Ionic (Protein Cationic) |
O31 | NH2 | ARG- 131 | 2.8 | 175.89 | H-Bond (Protein Donor) |
O32 | NH1 | ARG- 131 | 3.04 | 164.7 | H-Bond (Protein Donor) |
C6S | CE | MET- 208 | 3.53 | 0 | Hydrophobic |
C6S | CD1 | LEU- 213 | 3.3 | 0 | Hydrophobic |
CB2 | CE1 | PHE- 220 | 3.68 | 0 | Hydrophobic |
C3S | CZ | PHE- 222 | 4.47 | 0 | Hydrophobic |
C5S | CZ | PHE- 222 | 3.44 | 0 | Hydrophobic |
O11 | O | HOH- 6002 | 2.63 | 143.17 | H-Bond (Protein Donor) |
O31 | O | HOH- 6146 | 3.04 | 150.9 | H-Bond (Protein Donor) |
OE1 | O | HOH- 6356 | 3.32 | 137.33 | H-Bond (Protein Donor) |