Sandbox323: Difference between revisions

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4Q7Q is a homodimeric protein complex that originates from the bacterial species Chitinophaga Pinensis and has a mass of 58.5 kDa. It is a member of the SGNH Hydrolase Superfamily with structural and sequential similarities to esterases and lipases. Current evidence suggests it causes the hydrolysis of esters and/or acetyl groups on lipids/lipid-like molecules via a catalytic triad-like active site.
4Q7Q is a homodimeric protein complex that originates from the bacterial species Chitinophaga Pinensis and has a mass of 58.5 kDa. It is a member of the SGNH Hydrolase Superfamily with structural and sequential similarities to esterases and lipases. Current evidence suggests it causes the hydrolysis of esters and/or acetyl groups on lipids/lipid-like molecules via a catalytic triad-like active site.


<StructureSection load='4Q7Q' size='200' side='right' caption='3D Representation of 4Q7Q's structure' scene=''>
<load='4Q7Q' size='200' side='right' caption='3D Representation of 4Q7Q's structure' scene=''>


== Overview ==
== Overview ==
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The role of the chloride cofactor was not investigated thoroughly. Chloride ion was present in all reaction conditions, so it's independence was not tested. A future experiment would be testing the functionality of the enzyme without chloride in solution compared to with chloride ion.  
The role of the chloride cofactor was not investigated thoroughly. Chloride ion was present in all reaction conditions, so it's independence was not tested. A future experiment would be testing the functionality of the enzyme without chloride in solution compared to with chloride ion.  
</StructureSection>


== References ==
== References ==


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