| Description | 6-Phosphogluconate dehydrogenase ( ) (6PGD) is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP) [ , ]. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved []. The protein is a homodimer in which the monomers act independently []: each contains a large, mainly α-helical domain and a smaller β-α-β domain, containing a mixed parallel and anti-parallel 6-stranded β sheet []. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [].This signature, found in the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase, contains the 6-phosphogluconate binding site. The NAD-binding domain is described in . | Name | 6-phosphogluconate-binding site |
| Short Name | 6PGdom_BS | Type | Binding_site |
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