Sandbox Reserved 1677: Difference between revisions
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<scene name='87/873239/Nad_residues/1'>19 NAD+ Residues</scene> (binding site) | <scene name='87/873239/Nad_residues/1'>19 NAD+ Residues</scene> (binding site) | ||
''' Ile 155, Asn 159, Lys 182, Gly 219, Ile 233, Ser 236, Ala 239, leu 242, Glu 257, leu 258, Gly 259, Cys 291, Glu 391, Phe 393 == | ''' Ile 155, Asn 159, Lys 182, Gly 219, Ile 233, Ser 236, Ala 239, leu 242, Glu 257, leu 258, Gly 259, Cys 291, Glu 391, Phe 393 == | ||
Nicotinamide ring is helped in place by van der Waals interactions with Leu 258, Leu 419, and Phe 456 and a hydrogen bond from the backbone carbonyl of Leu 258 to the NH2 grouo of the cofactors. Polar interactions between the adenine ribose ring and side chains of Lys 182 and Glu 185 contribute to NAD+ binding. Interaction of Glu 185 with the 2' hydroxyl group of the adenine ribose determine the cofactor specificity as AldC is not able to accomodate the 2 phosphate of NADP(H) sterically. | |||
'''''' | '''''' | ||
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'''Trp 160 Tyr 163, Trp 450, Phe 456, Tyr 458, met 114, leu 118 =='''''' | '''Trp 160 Tyr 163, Trp 450, Phe 456, Tyr 458, met 114, leu 118 =='''''' | ||
Apolar interactions dominate the octanal binding in the hydrophobic substrate binding pocket. A cluster of aromatic residues and two nonpolar residues (Methionine and Leucine) peovides hydophobic environment that accommodates octanal and other aliphatic aldehydes. The substrate binding site forms an aromatic box for adaptable apolar ligand interaction. | |||
https://proteopedia.org/wiki/images/4/48/Screen_Shot_2021-04-18_at_4.03.57_PM.png | https://proteopedia.org/wiki/images/4/48/Screen_Shot_2021-04-18_at_4.03.57_PM.png | ||
<scene name='87/873239/View_of_active_site/2'>Active Site structure</scene>, | <scene name='87/873239/View_of_active_site/2'>Active Site structure</scene>, | ||
https://proteopedia.org/wiki/images/c/cc/Screen_Shot_2021-04-18_at_4.04.32_PM.png | https://proteopedia.org/wiki/images/c/cc/Screen_Shot_2021-04-18_at_4.04.32_PM.png | ||
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== Other important features == | == Other important features == | ||
The Rossmann fold of the NAD(H) binding domain provides extensive polar and apolar interactions that position the nicotinamide ring of NAD+ in proximity to the C291A point mutation. Its main function is to bind NAD+ cofactor and contribute to substrate binding. | |||
</StructureSection> | </StructureSection> | ||
