Sandbox Reserved 1805: Difference between revisions

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== Important amino acids==
== Important amino acids==
Amino acids involved in the catalytic triad for MqnA include N17, S86, and Y242. Other amino acids that help bind the main ligand through hydrophobic interactions include I13, N17, V18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, and Y242.  
Amino acids involved in the catalytic triad for MqnA include N17, S86, and Y242. Other amino acids that help bind the main ligand through hydrophobic interactions include I13, N17, V18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, and Y242. A view of just the ligan is shown
== Structural highlights ==
== Structural highlights ==
In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this <scene name='95/954102/Secondary_structure/1'>image</scene>, alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of <scene name='95/954102/Tertiary_structure/1'>tertiary structure</scene>,
In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this <scene name='95/954102/Secondary_structure/1'>image</scene>, alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of <scene name='95/954102/Tertiary_structure/1'>tertiary structure</scene>, we see two distinct lobes present in MqnA. In the image, it is clear just how much space is occupied by the atoms, making our catalytic triad tucked away and hidden. This demonstrates the importance of the venus flytrap fold that exposes our ligand for binding. Its change in conformation is absolutely vital for its function.