Histidinol-phosphate transaminase(HisC) is an enzyme used to catalyze the reaction between L-histidinol phoshpate and 2-oxoglutarate. HisC transfers an amino group. This enzyme can be found in the following organisms: thermotoga maritima, mycobacterium tuberculosis, and arabidopsis thaliana.
The structure of Histidinol-phosphate transaminase is depicted to the right. This image shows the secondary structure of the enzyme. The alpha helices are highlighted in light blue and the beta sheets are purple. Alpha helices and beta sheets are the two components that make up the secondary structure of the enzyme. Each of the spheres within the secondary structures is selenomethionine. The different colors represent the different elements that make up selenomethionine.
Source: Damodhran, L., S. K. Burley, and S. Swaminathan. "Crystal Structure of Histidinol-Phosphate Transaminase." RCSB Protein Data Bank. RCSB Protein Date Bank, n.d. Web. 06 Apr. 2014. <http://www.rcsb.org/pdb/explore/explore.do?structureId=3HDO>.
Damodhran, L., S. K. Burley, and S. Swaminathan. "Crystal Structure of Histidinol-Phosphate Transaminase." RCSB Protein Data Bank. RCSB Protein Date Bank, n.d. Web. 06 Apr. 2014. <http://www.rcsb.org/pdb/explore/explore.do?structureId=3HDO>.
