THEM2 Protein Crystal(CBCRY16)

Inquiry

Product Summary
Name	THEM2 Protein Crystal
	Download Datasheet
Cat No.	CBCRY16
Fragment	Full length
Protein Description	Thioesterase superfamily member 2
Background	The crystallographic structure of recombinant hTHEM2, determined by the single-wavelength anomalous dispersion method at 2.3A resolution, demonstrates that hTHEM2 indeed contains a hotdog-fold and forms a back-to-back tetramer as other hotdog proteins. Based on structural and sequence conservation, the thioesterase active site in hTHEM2 is predicted. The structure and substrate specificity are most similar to those of the bacterial phenylacetyl-CoA hydrolase. Asp65, located on the central alpha-helix of subunit B, was shown by site-directed mutagenesis to be essential to catalysis.
Protein Classification	Hydrolase
Structure Weight	132969.96 Da
Method	X-Ray Diffraction
Resolution	2.3Å
Ligand Chemical Component	sulfate ion
Reference	Cheng, Z., Song, F., Shan, X., Wei, Z., Wang, Y., Dunaway-Mariano, D., Gong, W. (2006) Crystal structure of human thioesterase superfamily member 2 Biochem.Biophys.Res.Commun. 349: 172-177

Online Inquiry

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.