1.900 Å
X-ray
2005-08-14
Name: | Histamine N-methyltransferase |
---|---|
ID: | HNMT_HUMAN |
AC: | P50135 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.1.1.8 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 36.779 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.154 | 1404.000 |
% Hydrophobic | % Polar |
---|---|
56.73 | 43.27 |
According to VolSite |
HET Code: | 2PM |
---|---|
Formula: | C17H22NO |
Molecular weight: | 256.363 g/mol |
DrugBank ID: | DB01075 |
Buried Surface Area: | 70.48 % |
Polar Surface area: | 13.67 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 1 |
H-Bond Donors: | 1 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
52.947 | -12.7122 | 30.2645 |
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 |
C3 | CD2 | LEU- 8 | 4.48 | 0 | Hydrophobic |
C10 | CB | TYR- 146 | 3.57 | 0 | Hydrophobic |
C14 | CH2 | TRP- 179 | 3.6 | 0 | Hydrophobic |
C7 | CZ2 | TRP- 183 | 3.98 | 0 | Hydrophobic |
C14 | CZ2 | TRP- 183 | 4.1 | 0 | Hydrophobic |
C10 | CB | CYS- 196 | 4.48 | 0 | Hydrophobic |
C11 | SG | CYS- 196 | 3.75 | 0 | Hydrophobic |
C12 | CE2 | TYR- 198 | 3.47 | 0 | Hydrophobic |
C14 | CE2 | PHE- 243 | 4.38 | 0 | Hydrophobic |
C2 | CE1 | PHE- 243 | 3.47 | 0 | Hydrophobic |
C4 | CB | GLU- 246 | 4.37 | 0 | Hydrophobic |
N1 | O | HOH- 653 | 2.73 | 157.37 | H-Bond (Ligand Donor) |