Sandbox Reserved 1805: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 15: | Line 15: | ||
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. | ||
== 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 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>, | ||