Sandbox Reserved 1697: Difference between revisions
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== Important amino acids== | == Important amino acids== | ||
In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. | In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313. | ||
== Structural highlights == | == Structural highlights == | ||
This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is 77% helix and 23% beta sheet, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. | |||
== Other important features == | == Other important features == | ||
