Sandbox Reserved 200: Difference between revisions

Similar to dimer, the structure of the monomer is conserved except for the <scene name='Sandbox_Reserved_200/Minor_trimer/2'>hinge loop</scene>.  The <scene name='Sandbox_Reserved_200/Minor_trimer/3'>active sites</scene> of the trimers are made up of the same amino acid residues as the monomers and dimers.  The trimer's active site is slightly different from that of the monomer and dimer because it has a sulfate ion trap.<ref name="liu01"/>  A total of four sulfate ions bind to the minor trimer, three to the active sites, and one to the hinge loop.  <scene name='Sandbox_Reserved_200/Minor_trimer/5'>Gly112</scene> residues from each subunit as well as other amino acid residues bind to the sulfate ion.  An intricate network of hydrogen bonding holds the sulfate ion in the trap. <ref name="liu01"/> The monomers and dimers also have sulfate ions bond to their active site, but the ions seem to have a stronger presence within the trimer.  The ions are bound to the active site are completely surrounded by water which is responsible for the <scene name='Sandbox_Reserved_200/Minor_trimer/7'>hydrogen bonding</scene> to the sulfate ion.