ATCase

	Select: Protein ATP All Rotate: X 90° X -90° Y 90° Y -90°	Distances: His20 Lys94 Lys60 Ile12 Reset The rotate buttons act on the entire structure. Remove the distance monitors with a second click.
	The ATP binding pocket with four "close" residues (<3.2 Å) shown as Ball & Stick. The van der Waals surface of the binding pocket (atoms within 5.5 Å of ATP) shown as Ball & Stick with dot surface. Aspartate Carbamoyltransferase Overall architecture of the regulatory subunit of aspartate carbamoyl-transferase (ATCase). The regulatory subunit is shown as Cartoons with Group coloring. The ligand (ATP) is Spacefill, colored CPK. Use the buttons to the right of the image to select portions of the structure for display or coloring in the Chime menu.

The coordinates are from 7at1.pdb (subunit B only). Gouaux, J. E. et al. (1990) "Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8 Å resolution and neutral pH."Biochemistry 29, 7702.

Additional notes on the ATCase structure:: Crystals grown at pH 7.; Resolution: 2.8 Å; R-factor: 0.17.