2.000 Å
X-ray
2006-09-23
Name: | Histone-lysine N-methyltransferase EHMT1 |
---|---|
ID: | EHMT1_HUMAN |
AC: | Q9H9B1 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 39.079 |
---|---|
Number of residues: | 28 |
Including | |
Standard Amino Acids: | 26 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.535 | 722.250 |
% Hydrophobic | % Polar |
---|---|
33.64 | 66.36 |
According to VolSite |
HET Code: | SAH |
---|---|
Formula: | C14H20N6O5S |
Molecular weight: | 384.411 g/mol |
DrugBank ID: | DB01752 |
Buried Surface Area: | 64.09 % |
Polar Surface area: | 212.38 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 10 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 1 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
63.9518 | 18.9109 | 4.21108 |
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 |
N | O | TRP- 1107 | 2.67 | 169.89 | H-Bond (Ligand Donor) |
OXT | N | TRP- 1107 | 2.94 | 146.46 | H-Bond (Protein Donor) |
SD | CE1 | TYR- 1142 | 3.73 | 0 | Hydrophobic |
O | OH | TYR- 1142 | 2.98 | 151.82 | H-Bond (Protein Donor) |
N | OD1 | ASN- 1169 | 2.83 | 143.1 | H-Bond (Ligand Donor) |
N7 | N | HIS- 1170 | 2.96 | 151.94 | H-Bond (Protein Donor) |
N6 | O | HIS- 1170 | 2.86 | 141.15 | H-Bond (Ligand Donor) |
C5' | CE2 | TYR- 1211 | 3.77 | 0 | Hydrophobic |
C3' | CE2 | TYR- 1211 | 4.47 | 0 | Hydrophobic |
C3' | CZ | PHE- 1215 | 3.94 | 0 | Hydrophobic |
N1 | N | ARG- 1226 | 2.9 | 153.38 | H-Bond (Protein Donor) |