The structure of the dengue virus 2'0 methyltransferase is shown in ribbons complexed with ribavirin 5' triphosphate in the forefront and s-adenosyl homocysteine in the background (PDB ID 1R6A). Ligands are shown in CPK and protein residues are shown in tube representation. Download Image
The human D3 dopamine receptor (PDB ID 3PBL) is shown in complex with D2R/D3R-specific antagonist eticlopride (shown in CPK). Active site residues are shown in ball-and-stick representation.The receptor surface illustrates the contour of the binding cavity. Download Image
Estrogen receptor beta (PDB ID 1X78) is shown in complex with two different ligands (gray and green) that interact with a nearby water molecule. The receptor structure is shown in ribbons colored according to residue position, and the binding site surface contour is shown in blue. Download Image
An inhibitor is shown buried in the active site of checkpoint kinase 1 (PDB ID 2ROU). The inhibitor is shown in CPK representation and water molecules are shown in ball-and-stick representation. Download Image
The human D3 dopamine receptor (PDB ID 3PBL) is shown in complex with D2R/D3R-specific antagonist eticlopride (shown in CPK). Active site residues are shown in ball-and-stick representation. The receptor surface is colored according to electrostatic potential using a rainbow spectrum. Download Image
The human A2A adenosine receptor is shown with a sub-type selective antagonist (PDB ID 3EML). Download Image
The human A2A adenosine receptor is shown with a sub-type selective antagonist (PDB ID 3EML). The binding site surface is shown colored according to electrostatic potential. Download Image
A nanomolar-potency agonist bound to the active site of the adenosine A2A receptor (PDB ID 3QAK), a GPCR target of considerable interest. Download Image
The structure of the dengue virus 2'0 methyltransferase is shown as a surface. Ribavirin 5' triphosphate is shown bound in the forefront and s-adenosyl homocysteine is shown bound in the background (PDB ID 1R6A). Download Image
