Sandbox Reserved 1665: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<scene name='87/873227/Secondary_structure/1'>Secondary structure</scene> has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein | <scene name='87/873227/Secondary_structure/1'>Secondary structure</scene> has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein | ||
<scene name='87/873227/Tertiary_structure_of_protein/2'>Tertiary Structure</scene> of protein shows alpha and beta sheets. | |||
In this <scene name='87/873227/Space_filled_view/1'>space filled view</scene> of the protein it show many amino acid residues that are hydrophobic (yellow) pushing away towards the binding sites because there are water molecules around them. Each chain of the protein shows a cleft for NAD and Octanal. We can tell there is a binding cleft for octanal because many amino residues like Trp 160, Tyr 163, Trp 450, Phe 456, and Tyr 468 provided a hydrophobic environment for this binding site. | In this <scene name='87/873227/Space_filled_view/1'>space filled view</scene> of the protein it show many amino acid residues that are hydrophobic (yellow) pushing away towards the binding sites because there are water molecules around them. Each chain of the protein shows a cleft for NAD and Octanal. We can tell there is a binding cleft for octanal because many amino residues like Trp 160, Tyr 163, Trp 450, Phe 456, and Tyr 468 provided a hydrophobic environment for this binding site. | ||
