THEM2 Protein Crystal(CBCRY16)
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| Product Summary | |
|---|---|
| Name | THEM2 Protein Crystal |
Download Datasheet
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| 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 |
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