Sandbox Reserved 470: Difference between revisions
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==Structure== | ==Structure== | ||
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GAPDH has two domains, a GAPDH-like, C-terminal domain, and an NAD Binding Domain. | *While GAPDH possesses four cysteine residues, its <scene name='Sandbox_Reserved_470/Active_site_gapdh/1'>active site</scene> is located around <scene name='Sandbox_Reserved_470/Cysteine_active_site/1'>Cysteine 149</scene>. | ||
*GAPDH has two domains, a GAPDH-like, C-terminal domain, and an NAD Binding Domain. | |||
:The <scene name='Sandbox_Reserved_470/Nad_binding_domain/3'>NAD (Nucleotide) Binding Domain </scene> is an Alpha Beta 3-Layer(α-β-α) Sandwich, including amino acids 1-138 and 301-340 on chains O and Q . Its [http://en.wikipedia.org/wiki/CATH CATH] reports a Rossmann fold and a classification as an [http://en.wikipedia.org/wiki/Oxidoreductase oxidoreductase]. | |||
:The <scene name='Sandbox_Reserved_470/Gapdh-like_c-terminal_domain/3'>GAPDH-like, C-terminal domain</scene>GAPDH-like, C-terminal domain (Catalytic domain) is an Alpha Beta 2-Layer(α-β) Sandwich, including amino acids 139 - 300 on chains O and Q . Its CATH reports a holo-D-Glyceraldehyde-3-Phosphate Dehydrogenase, (domain 2) and a classification as an oxidoreductase (aldehyde(D)-NAD(A)). | |||
*Depending on the environment, including variations in temperature and acidity, GAPDH can have different structural qualities and physical properties. In some cases, it is observed as a twinned structure with an α/β barrel. | |||
==Importance== | ==Importance== | ||
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