Sandbox Reserved 459: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Alisha Parks (talk | contribs) No edit summary |
Alisha Parks (talk | contribs) No edit summary |
||
| Line 23: | Line 23: | ||
---- | ---- | ||
To examine the crystal structure of human salivary amylase, X-ray crystallography was used with a resolution of 1.60 Å. The active site of alpha-amylase contains a trio of acidic groups that do most of the work. Ca2+ is a common <scene name='Sandbox_Reserved_459/Christie_ligand/1'>ligand</scene> for alpha amylase.The Ca2+ ion is bound to Asnl00, Arg158, Asp167, His201 and three water molecules. | |||
<scene name='Sandbox_Reserved_459/Christie_helix/1'>helices</scene> | <scene name='Sandbox_Reserved_459/Christie_helix/1'>helices</scene> | ||
<scene name='Sandbox_Reserved_459/Christie_beta_sheet/1'>beta strands</scene> | <scene name='Sandbox_Reserved_459/Christie_beta_sheet/1'>beta strands</scene> | ||
<scene name='Sandbox_Reserved_459/Christie_hydrophobic/1'>hydrophobic residues</scene> | <scene name='Sandbox_Reserved_459/Christie_hydrophobic/1'>hydrophobic residues</scene> | ||
== '''Mechanism of Action''' == | == '''Mechanism of Action''' == | ||
