Sandbox Reserved 1094: Difference between revisions

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  Each <scene name='82/829347/Monomerg6pd/1'>monomer</scene> is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/5'>1 red and 1 green</scene>.
  Each <scene name='82/829347/Monomerg6pd/1'>monomer</scene> is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/5'>1 red and 1 green</scene>.
Depending on several conditions, it can dimerize to form tetramers. Each monomer is composed of a small domain localized in the amino terminal part which constitute the coenzyme binding domain and a larger domain in the carboxy terminal part which constitute the substrate binding domain. the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+ using the Rossman fold.<ref name="struc">PMID: 7881907</ref>  
Depending on several conditions, it can dimerize to form tetramers. Each monomer is composed of a small domain localized in the amino terminal part which constitute the coenzyme binding domain and a larger domain in the carboxy terminal part which constitute the substrate binding domain. the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+ using the Rossman fold.<ref name="struc">PMID: 7881907</ref>  
''Coenzyme binding domain''
The coenzyme binding domain binds the [https://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide 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].