2.440 Å
X-ray
2008-08-25
Name: | Nitric oxide synthase, endothelial |
---|---|
ID: | NOS3_HUMAN |
AC: | P29474 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 1.14.13.39 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 34.947 |
---|---|
Number of residues: | 19 |
Including | |
Standard Amino Acids: | 15 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | CL |
Ligandability | Volume (Å3) |
---|---|
0.649 | 1839.375 |
% Hydrophobic | % Polar |
---|---|
49.36 | 50.64 |
According to VolSite |
HET Code: | 327 |
---|---|
Formula: | C10H15N2OS |
Molecular weight: | 211.304 g/mol |
DrugBank ID: | DB07001 |
Buried Surface Area: | 45.91 % |
Polar Surface area: | 75.08 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 2 |
Rings: | 2 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
23.4728 | 13.2376 | 22.6702 |
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 | CG | GLN- 213 | 4.25 | 0 | Hydrophobic |
S1 | CG | PRO- 300 | 3.6 | 0 | Hydrophobic |
C7 | CG2 | VAL- 302 | 3.67 | 0 | Hydrophobic |
C9 | CG2 | VAL- 302 | 4.25 | 0 | Hydrophobic |
N2 | O | TRP- 322 | 3.3 | 135.46 | H-Bond (Ligand Donor) |
N1 | OE1 | GLU- 327 | 2.73 | 172.39 | H-Bond (Protein Donor) |
N2 | OE2 | GLU- 327 | 2.74 | 169.51 | H-Bond (Ligand Donor) |
N2 | OE1 | GLU- 327 | 3.38 | 132.95 | H-Bond (Ligand Donor) |