2.100 Å
X-ray
1999-03-22
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 | 9 % |
B | 91 % |
B-Factor: | 21.553 |
---|---|
Number of residues: | 33 |
Including | |
Standard Amino Acids: | 31 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.783 | 911.250 |
% Hydrophobic | % Polar |
---|---|
40.74 | 59.26 |
According to VolSite |
HET Code: | GBX |
---|---|
Formula: | C30H26N3O9S |
Molecular weight: | 604.607 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 55.7 % |
Polar Surface area: | 245.77 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 10 |
H-Bond Donors: | 4 |
Rings: | 5 |
Aromatic rings: | 4 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
21.9323 | 5.42063 | 29.0517 |
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 |
C10 | CZ | TYR- 7 | 4.27 | 0 | Hydrophobic |
SG2 | CE1 | TYR- 7 | 3.41 | 0 | Hydrophobic |
CB2 | CE2 | PHE- 8 | 3.55 | 0 | Hydrophobic |
C5' | CB | PHE- 8 | 3.96 | 0 | Hydrophobic |
C6' | CB | PHE- 8 | 4.3 | 0 | Hydrophobic |
C6' | CG1 | VAL- 10 | 4.32 | 0 | Hydrophobic |
C5' | CG2 | VAL- 10 | 3.56 | 0 | Hydrophobic |
O12 | CZ | ARG- 13 | 3.95 | 0 | Ionic (Protein Cationic) |
O8 | NE | ARG- 13 | 2.95 | 165.85 | H-Bond (Protein Donor) |
C9 | CG | ARG- 13 | 3.4 | 0 | Hydrophobic |
CB1 | CD | ARG- 13 | 4.07 | 0 | Hydrophobic |
SG2 | CG | ARG- 13 | 4.15 | 0 | Hydrophobic |
C7' | CG1 | VAL- 35 | 4.36 | 0 | Hydrophobic |
O31 | NE1 | TRP- 38 | 3.19 | 145.75 | H-Bond (Protein Donor) |
O32 | NZ | LYS- 44 | 3.55 | 0 | Ionic (Protein Cationic) |
CG1 | CB | GLN- 51 | 4.16 | 0 | Hydrophobic |
O32 | NE2 | GLN- 51 | 2.64 | 161.03 | H-Bond (Protein Donor) |
O2 | N | LEU- 52 | 2.63 | 162.26 | H-Bond (Protein Donor) |
N2 | O | LEU- 52 | 2.59 | 150.18 | H-Bond (Ligand Donor) |
O11 | OG | SER- 65 | 3.39 | 146.02 | H-Bond (Protein Donor) |
O11 | N | SER- 65 | 2.91 | 159.78 | H-Bond (Protein Donor) |
O12 | OG | SER- 65 | 2.74 | 136.35 | H-Bond (Protein Donor) |
O12 | N | SER- 65 | 3.38 | 143.64 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 98 | 3.36 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 98 | 2.61 | 0 | Ionic (Ligand Cationic) |
N1 | OD2 | ASP- 98 | 2.61 | 146.71 | H-Bond (Ligand Donor) |
C7 | CE2 | TYR- 108 | 4.04 | 0 | Hydrophobic |
C11 | CZ | TYR- 108 | 3.29 | 0 | Hydrophobic |