Sandbox2O14: Difference between revisions
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2O14 is a monomeric protein complex that originates from the bacterial species Bacillus subtilis and has a mass of 41.79 kDa. Using InterPro this protein was assumed to be like Rhamnogalacturan acetylesterase, which falls under the SGNH Hydrolase Superfamily with structural and sequential similarities to lipases, esterases, along with similar functional domains to galactose-binding. With the research performed with current protein databases available, the evidence suggests that this protein removes acetyl groups from the backbone proteins by hydrolyzing the acetyl esters. It accomplishes this most likely through the catalytic triad of serine-histidine-aspartic acid. | 2O14 is a monomeric protein complex that originates from the bacterial species Bacillus subtilis and has a mass of 41.79 kDa. Using InterPro this protein was assumed to be like Rhamnogalacturan acetylesterase, which falls under the SGNH Hydrolase Superfamily with structural and sequential similarities to lipases, esterases, along with similar functional domains to galactose-binding. With the research performed with current protein databases available, the evidence suggests that this protein removes acetyl groups from the backbone proteins by hydrolyzing the acetyl esters. It accomplishes this most likely through the catalytic triad of serine-histidine-aspartic acid. | ||
<StructureSection load='2O14' size='400' side='right' caption='3D Representation of 2O14’s structure. | <StructureSection load='2O14' size='400' side='right' caption='3D Representation of 2O14’s structure.' scene=''> | ||
== Overview == | == Overview == | ||
