Sandbox Reserved 1094: Difference between revisions
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====''Coenzyme binding domain''==== | ====''Coenzyme binding domain''==== | ||
The coenzyme binding domain binds the [[NAD]] or [https://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide_phosphate NADP] which participes in the dehydrogenation of '''G6P'''. | The <scene name='82/829347/Domain_coenzyme2/1'>coenzyme binding domain</scene> binds the [[NAD]] or [https://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide_phosphate NADP] which participes in the dehydrogenation of '''G6P'''. | ||
It is defined by a typical [https://scop.berkeley.edu/sunid=30074 β-α-β dinucleotide-binding fold] corresponding to a [https://en.wikipedia.org/wiki/Rossmann_fold Rossman fold]. | It is defined by a typical [https://scop.berkeley.edu/sunid=30074 β-α-β dinucleotide-binding fold] corresponding to a [https://en.wikipedia.org/wiki/Rossmann_fold Rossman fold]. | ||
Only 17 residues over the total of 177 are strictly conserved some of them are involved in turns between some β strands and helices and the three last one of the domain are the first three residues of a strictly conserved nine-residue peptide. | Only 17 residues over the total of 177 are strictly conserved some of them are involved in turns between some β strands and helices and the three last one of the domain are the first three residues of a strictly conserved nine-residue peptide. | ||
<scene name='82/829347/Arg_46/ | <scene name='82/829347/Arg_46/2'>Arg46</scene> is strictlty conserved and involved in the binding with the 2'-phosphate of NADP. <scene name='82/829347/Gln_47/1'>Gln47</scene> could interact both with the 2'-phosphate of NADP or with the 2'-hydroxyl of NAD. | ||
====''Carboxyl terminus domain''==== | ====''Carboxyl terminus domain''==== | ||
The carboxyl terminus domain is defined by a β+α particular fold which has created his own fold family the [https://scop.berkeley.edu/sunid=39989 G6PD-like]. It is composed of a large essentially antiparallel curved nine-stranded β-sheet with 11 helices and remain well ordered to the carboxy-terminal residue. It is essential in the activity of the enzyme because it ensure the formation of the tertiary and the quaternary structure. | The <scene name='82/829347/Domain_cter2/1'>carboxyl terminus domain</scene> is defined by a β+α particular fold which has created his own fold family the [https://scop.berkeley.edu/sunid=39989 G6PD-like]. It is composed of a large essentially antiparallel curved nine-stranded β-sheet with 11 helices and remain well ordered to the carboxy-terminal residue. It is essential in the activity of the enzyme because it ensure the formation of the tertiary and the quaternary structure. | ||
====''Domain boundary''==== | ====''Domain boundary''==== | ||
