Sandbox Reserved 428: Difference between revisions

Protein 1db1 is found to complex with 1,25 Dihydroxy <scene name='48/483885/Vitamin_d3/1'>Vitamin D3</scene>. This molecule has three notable alcohol groups shown in red. Oxygen is electronegative,  giving alcohols the ability to participate in hydrogen bonding with the protein. Vitamin D3 has a large number of relations with the residues on the protein chain. First in the sequence are <scene name='48/483885/Residues_140-151/2'>residues 140-151</scene>. Tyr143, shown in blue, is the closest to the ligand at 2.83 angstroms. This is sightly large but there is still the possibility of hydrogen bonding. Tyr147 in green and Phe150 in black are also known to have interactions with Vitamin D3 they are farther away and therefore less significant. Next down the peptide chain are <scene name='48/483885/Residues_235-240/1'>residues 235-240</scene>. Ser237, shown in green, has significant  interactions with vitamin D3 this can be seen by its short distance 2.78 angstroms. Only 40 residues away, more hydrogen bonding is occurring.<scene name='48/483885/Residues_270-280/1'>Arg274 and Ser278</scene> form bonds with the same oxygen atoms as Tyr143 and Ser237 respectively. This means that the oxygen atoms of vitamin D3, when bound to the receptor, are negatively charged and stabilized by protons. On the opposite end of vitamin D3 there is an additional negatively charged oxygen. Although this oxygen does not participate in hydrogen bonding. <scene name='48/483885/His305_and_his397/1'>His305 and His397</scene>, shown in blue and green respectively, Contain aromatic rings. These rings are able to momentarily accept the electrons donated by the oxygen because they can delocalize the charge. This creates two pseudo-covalent bonds that is approximately 2.81 angstroms.