Sandbox Reserved 1102: Difference between revisions

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5y6n is a 1 chain protein of 438 residues.

There are 2 main activities: ATP binding and helicase activity.

Helicase from Zika virus with a specific domain : a serine protease. It is a specific class of protein that hydrolysis peptide bonds from proteins.

The helicase active site has a serine residue that serves as a nucleophilic amino acid. This residue is essential for the catalytic activity of the enzyme.The serine protases present a catalytic triad composed of 3 amino acids His57 Asp102 and Ser195.These 3 amino acids interaction is due to the folding of the protein ~~and~~ allows to cleave the substrate by attacking its carbonyl group.

There are two ligands: ADP and Manganese II ion

The helicase active site has a serine residue that serves as a nucleophilic amino acid. This residue is essential for the catalytic activity of the enzyme.The serine protases present a catalytic triad composed of 3 amino acids His57 Asp102 and Ser195.These 3 amino acids have a specific interaction which is due to the folding of the protein. The tridimentional conformation of the protein brings closer these 3 residues. Their side chains have a specific function :

Ser195: the hydroxyl group plays the role of a nucleophile that attack the substrate.

His57: the nitrogen receives an hydrogen from the hydroxyl group of Ser195.

Asp102: this amino acid allows to increase the electronegativity of His157 nitrogen by making hydrogen bond with His157.

All these reactions allows to cleave the substrate by attacking its carbonyl group.

There are two ligands for zika helicase : ADP and Manganese II ion

ADP

Manganese II ion

== References ==

Sandbox Reserved 1102: Difference between revisions

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@@ Line 40: / Line 40: @@
 y6n is a 1 chain protein of 438 residues.
 There are 2 main activities: ATP binding and helicase activity.
 Helicase from Zika virus with a specific domain : a serine protease. It is a specific class of protein that hydrolysis peptide bonds from proteins.
-The helicase active site has a serine residue that serves as a nucleophilic amino acid. This residue is essential for the catalytic activity of the enzyme.The serine protases present a catalytic triad composed of 3 amino acids His57 Asp102 and Ser195.These 3 amino acids interaction is due to the folding of the protein and allows to cleave the substrate by attacking its carbonyl group.
-There are two ligands: ADP and Manganese II ion
+The helicase active site has a serine residue that serves as a nucleophilic amino acid. This residue is essential for the catalytic activity of the enzyme.The serine protases present a catalytic triad composed of 3 amino acids His57 Asp102 and Ser195.These 3 amino acids have a specific interaction which is due to the folding of the protein. The tridimentional conformation of the protein brings closer these 3 residues. Their side chains have a specific function :
+Ser195: the hydroxyl group plays the role of a nucleophile that attack the substrate.
+His57: the nitrogen receives an hydrogen from the hydroxyl group of Ser195.
+Asp102: this amino acid allows to increase the electronegativity of His157 nitrogen by making hydrogen bond with His157.
+All these reactions allows to cleave the substrate by attacking its carbonyl group.
+There are two ligands for zika helicase : ADP and Manganese II ion
+ ADP
+ Manganese II ion
 == References ==
 <references/>